Publications

Selected publications since 1995

2020

Tomiczek B, Delewski W, Nierzwicki L, Stolarska M, Grochowina I, Schilke B, Dutkiewicz R, Uzarska MA, Ciesielski SJ, Czub J, Craig EA and Marszalek J.
Two-step mechanism of J-domain action in driving Hsp70 function.
PLoS Comput Biol. 2020 16(6):e1007913. DOI: 10.1371/journal.pcbi.1007913. [PubMed]

Kleczewska M, Grabinska A, Jelen M, Stolarska M, Schilke B, Marszalek J, Craig EA and Dutkiewicz R.
Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.
Int J Mol Sci. 2020 21(9). DOI: 10.3390/ijms21093326. [PubMed]

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2015 - 2019

2019

Shrestha OK, Sharma R, Tomiczek B, Lee W, Tonelli M, Cornilescu G, Stolarska M, Nierzwicki L, Czub J, Markley JL, Marszalek J, Ciesielski SJ and Craig EA.
Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.
PLoS One. 2019;14(5):e0217098. DOI: 10.1371/journal.pone.0217098. [PubMed]

2018

Craig EA.
Hsp70 at the membrane: driving protein translocation.
BMC Biol. 2018 16(1):11. DOI: 10.1186/s12915-017-0474-3. [PubMed]

2017

Schilke BA, Ciesielski SJ, Ziegelhoffer T, Kamiya E, Tonelli M, Lee W, Cornilescu G, Hines JK, Markley JL and Craig EA.
Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.
PLoS Genet. 2017 13(10):e1007084. DOI: 10.1371/journal.pgen.1007084. [PubMed]

Dutkiewicz R, Nowak M, Craig EA and Marszalek J.
Fe-S Cluster Hsp70 Chaperones: The ATPase Cycle and Protein Interactions.
Methods Enzymol. 2017 595:161-184. DOI: 10.1016/bs.mie.2017.07.004. [PubMed]

Craig EA and Marszalek J.
How Do J-Proteins Get Hsp70 to Do So Many Different Things?
Trends Biochem Sci. 2017 42(5):355-368. DOI: 10.1016/j.tibs.2017.02.007. [PubMed]

Ting SY, Yan NL, Schilke BA and Craig EA.
Dual interaction of scaffold protein Tim44 of mitochondrial import motor with channel-forming translocase subunit Tim23.
Elife. 2017 6. DOI: 10.7554/eLife.23609. [PubMed]

Ciesielski SJ and Craig EA.
Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism.
Curr Genet. 2017 63(1):51-56. DOI: 10.1007/s00294-016-0618-y. [PubMed]

2016

Liu Q and Craig EA.
Molecular biology: Mature proteins braced by a chaperone.
Nature. 2016 539(7629):361-362. DOI: 10.1038/nature20470. [PubMed]

Lee K, Sharma R, Shrestha OK, Bingman CA and Craig EA.
Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.
Nat Struct Mol Biol. 2016 23(11):1003-1010. DOI: 10.1038/nsmb.3299 [PubMed]

Yonashiro R, Tahara EB, Bengtson MH, Khokhrina M, Lorenz H, Chen KC, Kigoshi-Tansho Y, Savas JN, Yates JR, Kay SA, Craig EA, Mogk A, Bukau B and Joazeiro CA.
The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation.
Elife. 2016 5:e11794. DOI: 10.7554/eLife.11794 [PubMed]

Ciesielski SJ, Schilke B, Marszalek J and Craig EA.
Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation.
Mol Biol Cell. 2016 27(7):1060-1068. DOI: 10.1091/mbc.E15-12-0815 [PubMed]

Delewski W, Paterkiewicz B, Manicki M, Schilke B, Tomiczek B, Ciesielski SJ, Nierzwicki L, Czub J, Dutkiewicz R, Craig EA and Marszalek J.
Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein Interaction.
Mol Biol Evol. 2016 33(3):643-656. DOI: 10.1093/molbev/msv254 [PubMed]

2015

Schmitz-Abe K, Ciesielski SJ, Schmidt PJ, Campagna DR, Rahimov F, Schilke BA, Cuijpers M, Rieneck K, Lausen B, Linenberger ML, Sendamarai AK, Guo C, Hofmann I, Newburger PE, Matthews D, Shimamura A, Snijders PJ, Towne MC, Niemeyer CM, Watson HG, Dziegiel MH, Heeney MM, May A, Bottomley SS, Swinkels DW, Markianos K, Craig EA and Fleming MD.
Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9.
Blood. 2015 126(25):2734-2738. DOI: 10.1182/blood-2015-09-659854 [PubMed]

Yu HY, Ziegelhoffer T and Craig EA.
Functionality of Class A and Class B J-protein co-chaperones with Hsp70.
FEBS Lett. 2015 589(19 Pt B):2825-2830. DOI: 10.1016/j.febslet.2015.07.040 [PubMed]

Yu HY, Ziegelhoffer T, Osipiuk J, Ciesielski SJ, Baranowski M, Zhou M, Joachimiak A and Craig EA.
Roles of Intramolecular and Intermolecular Interactions in Functional Regulation of the Hsp70 J-portein Co-chaperone Sis1.
J Mol Biol. 2015 427(7):1632-1643. DOI: 10.1016/j.jmb.2015.02.007 [PubMed]

Kaschner LA, Sharma R, Shrestha OK, Meyer AE and Craig EA.
A conserved domain important for association of eukaryotic J-protein co-chaperones Jjj1 and Zuo1 with the ribosome.
Molecular Cell Research. Biochim Biophys Acta. 2015 1853(5):1035-1045. DOI: 10.1016/j.bbamcr.2015.01.014 [PubMed]

2010 - 2014

2014

Manicki, M., Majewska, J., Ciesielski, S., Schilke, B., Blenska, A., Kominek, J., Marszalek, J., Craig, E.A. and Dutkiewicz, R.
Overlapping Binding Sites of the Frataxin Homologue Assembly Factor and the Heat Shock Protein 70 Transfer Factor on the Isu Iron-sulfur Cluster Scaffold Protein.
J Biol Chem. 2014 289:30268-30278. DOI: 10.1074/jbc.M114.596726 [PubMed]

Ting, S.Y., Schilke, B.A., Hayashi, M. and Craig, E.A.
Architecture of the TIM23 Inner Mitochondrial Translocon and Interactions with the Matrix Import Motor.
J Biol Chem. 2014 289:28689-28696. DOI: 10.1074/jbc.M114.588152 [PubMed]

Craig, E.A. and Marszalek, J.
Yeast Hsp70 and J-protein Chaperones: Function and Interaction Network.
In: Houry WA, editor. The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Heidelberg: Springer Science and Business Media. 2014 Chapter 3, 53-82p [Springer]

2013

Kominek, J., Marszalek, J., Neuveglise, C., Craig, E.A. and Williams, B.L.
The complex evolutionary dynamics of Hsp70s: A genomic and functional perspective.
Genome Biol Evol. 2013 5:2460-2477. DOI: 10.1093/gbe/evt192 [PubMed]

Majewska, J., Ciesielski, S.J., Schilke, B., Kominek, J., Blenska, A., Delewski, W., Song, J-Y., Marszalek, J., Craig, E.A. and Dutkiewicz, R.
Binding of chaperone Jac1 and cysteine-desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu is mutually exclusive.
J Biol Chem. 2013 288:29134-29142. DOI: 10.1074/jbc.M113.503524 [PubMed]

Sahi, C., Kominek, J., Ziegelhoffer, T., Yu, H.Y., Baranowski, M., Marszalek, J. and Craig, E.A.
Sequential Duplications of an Ancient Member of the DnaJ-family Expanded the Functional Chaperone Network in the Eukaryotic Cytosol.
Mol Biol Evol. 2013 30:985-998. DOI: 10.1093/molbev/mst008 [PubMed]

Ciesielski, G.L. Plotka, M., Manicki, M., Schilke, B.A., Dutkiewicz, R., Sahi, C., Marzalek, J. and Craig, E.A.
Nucleoid localization of Hsp40 Mdj1 is important for its function in maintenance of mitochondrial DNA.
Biochim Biophys Acta-Molecular Cell Research. 2013 1833:2233-2243. DOI: 10.1016/j.bbamcr.2013.05.012 [PubMed]

2012

Ducett, J.K., Peterson, F.C., Hoover, L.A., Prunuske, A.J., Volkman, B.F., and Craig, E.A.
Unfolding of the C-Terminal Domain of the J-Protein Zuo1 Releases Autoinhibition and Aactivates Pdr1-Dependent Transcription.
J Mol Biol. 2012 425:19-31. DOI: 10.1016/j.jmb.2012.09.020 [PubMed]

Song, J-Y., Marszalek, J., and Craig, E.A.
The Cysteine desulfurase Nfs1 and Pim1 protease control levels of Isu, the FE-S cluster biogenesis scaffold.
Proc Natl Acad Sci USA. 2012 109:10370-10375. DOI: 10.1073/pnas.1206945109 [PubMed]

Prunuske, A., Waltner, J., Kuhn, P., and Craig, E.A.
Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1.
Proc Natl Acad Sci USA. 2012 109:472-477. DOI: 10.1073/pnas.1119184109 [PubMed]

Ciesielski, S.J., Schilke, B., Osipiuk, J., Bigelow, L., Mulligan, R., Majawska, J., Joachimiak, A., Marzalek, J., Craig, E.A., and Dutkiewicz, R.
Interaction of J-protein co-chaperone Jac1 with FE-S scaffold Isu is indispensible in vivo and conserved in evolution.
J Mol Biol. 2012 417:1-12. DOI: 10.1016/j.jmb.2012.01.022 [PubMed]

Schilke,  B.A., Hayashi, M., Craig, E.A.
Genetic analysis of complex interactions amongst components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.
Genetics. 2012 190:1341-1353. DOI: 10.1534/genetics.112.138743 [PubMed]

2011

Hines, J., Higurashi, T., Srinivasan, M., and Craig, E.A.
Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements.
Prion. 2011 5:238-244. DOI: 10.4161/pri.17818 [PubMed]

Hines, J. and Craig, E.A.
The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity.
Prion. 2011 5:164-168. DOI: 10.4161/pri.5.3.16895 [PubMed]

Pais, J.E., Schilke, B., and Craig, E.A.
Re-evaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.
Mol Biol Cell. 2011 22:4740-4749.DOI: 10.1091/mbc.E11-08-0715 [PubMed]

Hayashi, M., Schilke, B., Marszalek, J., Williams, B., and Craig, E.A.
Ancient gene duplication provided a key molecular step for anaerobic growth of baker’s yeast.
Mol Biol Evol. 2011 28:2005-2017. DOI: 10.1093/molbev/msr019 [PubMed]

Hines, J., Li, X., Du, Z., Higurashi, T., Li, L., and Craig, E.A.
[SWI+] the Prion Formed by the Chromatin Remodeling Factor Swi1 is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity.
PLoS Genet. 2011 7(2): e1001309. DOI: 10.1371/journal.pgen.1001309 [PubMed]

Craig, E.A and Marszalek, J.
Hsp70 chaperones. In: Encyclopedia of Life Sciences, 2011 John Wiley & Sons, Ltd., Chichester, UK, http://www.els.net/ [DOI: 10.1002/9780470015902.a0023188]. [PDF]

2010

Kampinga, H.H. and E.A. Craig.
The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Nat. Rev. Mol. Cell Biol. 2010 11:579-592. DOI: 10.1038/nrm2941 [PubMed]

Pukszta, S., Schilke, B., Dutkiewicz, R., Kominek, J., Moczulska, K., Stepien, B., Reitenga, K.G., Buknicki, J.M., Williams, B., Craig, E.A., and Marszalek, J.
Co-evolution driven switch of J-protein specificity toward an Hsp70 partner.
EMBO Rep. 2010 11:360-365. DOI: 10.1038/embor.2010.29 [PubMed]

Correia, A.R., Wang, T., Craig, E.A. and Gomes, C.M.
Iron binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region.
Biochem J. 2010 426:197-203. DOI: 10.1042/BJ20091612 [PubMed]

2005 - 2009

2009

Sahi, C., Lee, T., Inada, M., Pleiss, J.A., and Craig, E.A.
Cwc23, an Essential J Protein Critical for Pre-mRNA Splicing with a Dispensable J Domain.
Mol Cell Biol. 2009 30:33-42. DOI: 10.1128/MCB.00842-09. [PDF]

Meyer, A.E., Hoover, L.A., and Craig, E.A.
The Cytosolic J-protein, Jjj1, and Rei1 Function in the Removal of the Pre-60S Subunit Factor Arx1.
J. Biol. Chem. 2009 285:961-968. DOI: 10.1074/jbc.M109.038349. [PDF]

Weeks, S.A., Shield, W.P., Sahi, C., Craig, E.A., Rospert, S., and Miller, D.J.
A Targeted Analysis of Cellular Chaperones Reveals Contrasting Roles for Heat Shock Protein 70 in Flock House Virus RNA Replication.
J. Virol. 2009 84:330-339. DOI: 10.1128/JVI.01808-09. [PDF]

2008

Andrew AJ, Song J-Y, Schilke B, and Craig EA.
Postranslational Regulation of the Scaffold for FE-S cluster Biogenesis, Isu.
Mol. Biol. Cell. 2008 19:5259-5266. DOI: 10.1091/mbc.e08-06-0622. [PDF]

Higurashi T, Hines JK, Sahi C, Aron R, and Craig EA.
Specificity of the J-Protein SIS1 in the Propagation of Three Yeast Prions.
Proc Natl Acad Sci USA. 2008 105:16596-16601. DOI: 10.1073/pnas.0808934105. [PDF]

Schiller D, Cheng YC, Liu Q, Walter W, Craig EA.
Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mtHsp70 tethering.
Mol Cell Biol. 2008 28(13):4424-33. DOI: 10.1128/MCB.00007-08. [PDF]

Wang T, Craig, EA.
Binding of Yeast Frataxin to the Scaffold for Fe-S Cluster Biogenesis, Isu.
J Biol Chem. 2008 283(18):12674-9. DOI: 10.1074/jbc.M800399200. [PDF]

D’Silva PR, Schilke B, Hayashi M, Craig EA.
Interaction of the j-protein heterodimer pam18/pam16 of the mitochondrial import motor with the translocon of the inner membrane.
Mol Biol Cell. 2008 19(1):424-32. DOI: 10.1091/mbc.e07-08-0748. [PDF]

2007

Aron R, Higurashi T, Sahi C, Craig EA.
J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation.
EMBO J. 2007 26(16):3794-803. DOI: 10.1038/sj.emboj.7601811. [PDF]

Sahi C, Craig EA.
Network of general and specialty J protein chaperones of the yeast cytosol.
Proc Natl Acad Sci U S A. 2007 104(17):7163-8. DOI: 10.1073/pnas.0702357104. [PDF]

Meyer AE, Hung NJ, Yang P, Johnson AW, Craig EA
The specialized cytosolic J-protein, Jjj1, functions in 60S ribosomal subunit biogenesis.
Proc Natl Acad Sci U S A. 2007 104(5):1558-63. DOI: 10.1073/pnas.0610704104. [PDF]

2006

Schilke B, Williams B, Knieszner H, Pukszta S, D’Silva P, Craig EA, Marszalek J.
Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis.
Curr Biol. 2006 16(16):1660-5. DOI: 10.1016/j.cub.2006.06.069. [PDF]

Andrew AJ, Dutkiewicz R, Knieszner H, Craig EA, Marszalek J.
Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p.
J Biol Chem. 2006 281(21):14580-7. DOI: 10.1074/jbc.M600842200. [PDF]

Dutkiewicz R, Marszalek J, Schilke B, Craig EA, Lill R, Mühlenhoff U.
The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p.
J Biol Chem. 2006 281(12):7801-8. DOI: 10.1074/jbc.M513301200. [PDF]

Craig EA, Huang P, Aron R, Andrew A.
The diverse roles of J-proteins, the obligate Hsp70 co-chaperone.
Rev Physiol Biochem Pharmacol. 2006 156:1-21. Review. DOI: 10.1007/s10254-005-0001-0. [PDF]

2005

D’Silva P, Marszalek J, Craig EA.
An essential connection: link between Hsp70’s domains at last.
Mol Cell. 2005 20(4):493-4. DOI: 10.1016/j.molcel.2005.11.007. [PDF]

D’Silva PR, Schilke B, Walter W, Craig EA.
Role of Pam16’s degenerate J domain in protein import across the mitochondrial inner membrane.
Proc Natl Acad Sci U S A. 2005 102(35):12419-24. DOI: 10.1073/pnas.0505969102. [PDF]

Rauch T, Hundley HA, Pfund C, Wegrzyn RD, Walter W, Kramer G, Kim SY, Craig EA, Deuerling
Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli.
Mol Microbiol. 2005 57(2):357-65.  DOI: 10.1111/j.1365-2958.2005.04690.x. [PDF]

Knieszner H, Schilke B, Dutkiewicz R, D’Silva P, Cheng S, Ohlson M, Craig EA, Marszalek J.
Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold Isu.
J Biol Chem. 2005 280(32):28966-72. DOI: 10.1074/jbc.M503031200. [PDF]

Huang P, Gautschi M, Walter W, Rospert S, Craig EA.
The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.
Nat Struct Mol Biol. 2005 12(6):497-504. DOI: doi: 10.1038/nsmb942. [PDF]

Hundley HA, Walter W, Bairstow S, Craig EA.
Human Mpp11 J protein: Ribosome-Tethered Molecular Chaperones Are Ubiquitous.
Science. 2005 308(5724):1032-4. DOI: 10.1126/science.1109247. [PDF]

Aron R, Lopez N, Walter W, Craig EA, Johnson J.
In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae.
Genetics. 2005 169(4):1873-82. DOI: 10.1534/genetics.104.037242. [PDF]

Kim SY, Craig EA
Broad Sensitivity of Saccharomyces cerevisiae Lacking Ribosome-Associated Chaperone Ssb or Zuo1 to Cations, Including Aminoglycosides.
Eukaryot Cell. 2005 4(1):82-9. DOI: 10.1128/EC.4.1.82-89.2005. [PDF]

2000 - 2004

2004

D’Silva P, Liu Q, Walter W, Craig EA.
Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.
Nat Struct Mol Biol. 2004 11(11):1084-91. DOI: 10.1038/nsmb846. [PDF]

Aloria K, Schilke B, Andrew A, Craig EA.
Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo.
EMBO Rep. 2004 5(11):1096-101. DOI: 10.1038/sj.embor.7400272. [PDF]

Eisenman HC, Craig EA.
Activation of pleiotropic drug resistance by the J-protein and Hsp70-related proteins, Zuo1 and Ssz1.
Mol Microbiol. 2004 53(1):335-44. DOI: 10.1111/j.1365-2958.2004.04134.x. [PDF]

Loar JW, Seiser RM, Sundberg AE, Sagerson HJ, Ilias N, Zobel-Thropp P, Craig EA, Lycan DE.
Genetic and biochemical interactions among Yar1, Ltv1 and Rps3 define novel links between environmental stress and ribosome biogenesis in Saccharomyces cerevisiae.
Genetics. 2004 168(4):1877-89. DOI: 10.1534/genetics.104.032656. [PDF]

Dutkiewicz R, Schilke B, Cheng S, Knieszner H, Craig EA, Marszalek J.
Sequence specific interactions between mitochondrial Fe/S scaffold protein Isu1 and Hsp70 Ssq1 is essential for their in vivo function.
J Biol Chem. 2004 279(28):29167-74. DOI: 10.1074/jbc.M402947200. [PDF]

Craig EA, Huang P.
Cellular Functions of Hsp70 chaperones.
In: Kiefhaber T, Buchner J, editors. Handbook of Protein FoldingHeidelberg: Wiley Publishers; 2004. 490-515p.

2003

Craig EA.
Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins.
Curr Biol. 2003 13(23):R904-5. Review. DOI: 10.1016/j.cub.2003.11.009. [PDF]

D’Silva PD, Schilke B, Walter W, Andrew A, Craig EA.
J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix.
Proc Natl Acad Sci (USA). 2003 100(24):13839-44. DOI: 0.1073/pnas.1936150100. [PDF]

Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J.
Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.
J Biol Chem. 2003 278(32):29719-27. DOI: 10.1074/jbc.M303527200. [PDF]

Craig EA, Eisenman HC, Hundley HA.
Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding?
Curr Opin Microbiol. 2003 6(2):157-62. Review. DOI: 10.1016/s1369-5274(03)00030-4. [PDF]

Liu Q, D’Silva P, Walter W, Marszalek J, and Craig EA.
Regulated cycling of mitochondrial Hsp70 at the protein import channel.
Science 2003 300:139-41. DOI: 10.1126/science.1083379. [PDF]

Lopez, N, Aron, R and Craig, EA
Specificity of the Class II Hsp40 Sis1 in maintenance of the yeast prion [RNQ+]
Mol. Biol. Cell 2003 14:1172-81. DOI: 10.1091/mbc.e02-09-0593. [PDF]

2002

Craig EA, Marszalek J.
A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers.
Cell Mol Life Sci. 2002 59(10):1658-65. DOI: 10.1007/pl00012493. [PDF]

Johnson JL, Craig EA.
Identifying functional interactions with molecular chaperones.
Methods Enzymol. 2002 351:442-53. DOI: 10.1016/s0076-6879(02)51863-2. [PDF]

Carr-Schmid A, Pfund C, Craig EA, Kinzy TG.
Novel G-protein complex whose requirement is linked to the translational status of the cell.
Mol Cell Biol. 2002 22(8):2564-74. DOI: 10.1128/mcb.22.8.2564-2574.2002. [PDF]

Hundley H, Eisenman H, Walter W, Evans T, Hotokezaka Y, Wiedmann M, Craig E.
The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain.
Proc Natl Acad Sci U S A. 2002 99(7):4203-8. DOI: 10.1073/pnas.062048399. [PDF]

2001

Pfund C, Huang P, Lopez-Hoyo N, Craig EA.
Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.
Mol Biol Cell. 2001 12(12):3773-82. DOI: 10.1091/mbc.12.12.3773. [PDF]

Sondheimer, N, Lopez, N, Craig, EA and Lindquist, S.
The role of Sis1 in the maintenance of the [RNQ+] prion.
EMBO J, 2001 20:2435-42. DOI: 10.1093/emboj/20.10.2435. [PDF]

Johnson JL, Craig EA.
An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae.
J Cell Biol. 2001 152(4):851-6. DOI: 10.1083/jcb.152.4.851. [PDF]

Voisine C, Cheng YC, Ohlson M, Schilke B, Hoff K, Beinert H, Marszalek J, Craig EA.
Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.
Proc Natl Acad Sci U S A. 2001 98(4):1483-8. DOI: 10.1073/pnas.98.4.1483. [PDF]

Hon T, Lee HC, Hach A, Johnson JL, Craig EA, Erdjument-Bromage H, Tempst P, Zhang L.
The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.
Mol Cell Biol. 2001 21(23):7923-32. DOI: 10.1128/MCB.21.23.7923-7932.2001. [PDF]

Horton LE, James P, Craig EA, Hensold JO.
The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.
J Biol Chem. 2001 276(17):14426-33. DOI: 10.1074/jbc.M100266200. [PDF]

Liu Q, Krzewska J, Liberek K, Craig EA.
Mitochondrial Hsp70 Ssc1: role in protein folding.
J Biol Chem. 2001 276(9):6112-8. DOI: 10.1074/jbc.M009519200. [PDF]

Pfund C, Yan W, Craig EA.
The roles of the major cytoplasmic chaperones in normal eukaryotic cell growth: Hsc70 and its cofactors.
In: Lund P, editor. Molecular Chaperones in the Cell New York, NY: Oxford University Press. 2001. 119-137p.

2000

Bukau B, Deuerling E, Pfund C, Craig EA.
Getting newly synthesized proteins into shape.
Cell. 2000 101(2):119-22. DOI: 10.1016/S0092-8674(00)80806-5. [PDF]

Voisine C, Schilke B, Ohlson M, Beinert H, Marszalek J, Craig EA.
Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1.
Mol Cell Biol. 2000 20(10):3677-84. DOI: 10.1128/mcb.20.10.3677-3684.2000. [PDF]

Satyanarayana C, Schröder-Köhne S, Craig EA, Schu PV, Horst M.
Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole.
FEBS Lett. 2000 470(3):232-8. DOI: 10.1016/s0014-5793(00)01324-7. [PDF]

Johnson JL, Craig EA.
A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast.
Mol Cell Biol. 2000 20(9):3027-36. DOI: 10.1128/mcb.20.9.3027-3036.2000. [PDF]

1995 - 1999

1999

Craig EA, Voisine C, Schilke B.
Mitochondrial iron metabolism in the yeast Saccharomyces cerevisiae.
Biol Chem. 1999 380(10):1167-73. DOI: 10.1515/BC.1999.148. [PubMed]

Yan W, Craig EA.
The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.
Mol Cell Biol. 1999 19(11):7751-8. DOI: 10.1128/mcb.19.11.7751. [PDF]

Schilke B, Voisine C, Beinert H, Craig E.
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae.
Proc Natl Acad Sci U S A. 1999 96(18):10206-11. DOI: 10.1073/pnas.96.18.10206. [PDF]

Davis JE, Voisine C, Craig EA.
Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.
Proc Natl Acad Sci U S A. 1999 96(16):9269-76. DOI: 10.1073/pnas.96.16.9269. [PDF]

Voisine C, Craig EA, Zufall N, von Ahsen O, Pfanner N, Voos W.
The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70.
Cell. 1999 97(5):565-74. DOI: 10.1016/s0092-8674(00)80768-0. [PDF]

Lopez N, Halladay J, Walter W, Craig EA.
SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes.
J Bacteriol. 1999 181(10):3136-43. DOI: 10.1128/JB.181.10.3136-3143.1999. [PDF]

Sakuragi S, Liu Q, Craig E.
Interaction between the nucleotide exchange factor Mge1 and the mitochondrial Hsp70 Ssc1.
J Biol Chem. 1999 274(16):11275-82. DOI: 10.1074/jbc.274.16.11275. [PDF]

Shulga N, James P, Craig EA, Goldfarb DS.
A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport.
J Biol Chem. 1999 274(23):16501-7. DOI: 10.1074/jbc.274.23.16501. [PDF]

Craig EA, Yan W, James P.
Genetic Dissection of the yeast Hsp70 chaperone system.
In: Bukau B, editor. Molecular Chaperones and Folding Catalysts Amsterdam, NL: Harwood Academic Publishers; 1999. 139-162p.

1998

Lopez-Buesa P, Pfund C, Craig EA.
The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains.
Proc Natl Acad Sci U S A. 1998 95(26):15253-8. DOI: 10.1073/pnas.95.26.15253. [PDF]

Baxter BK, Craig EA.
Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.
J Bacteriol. 1998 180(24):6484-92. DOI: 10.1128/JB.180.24.6484-6492.1998. [PDF]

Yan W, Schilke B, Pfund C, Walter W, Kim S, Craig EA.
Zuotin, a ribosome-associated DnaJ molecular chaperone.
EMBO J. 1998 17(16):4809-17. DOI: 10.1093/emboj/17.16.4809. [PDF]

Pfund C, Lopez-Hoyo N, Ziegelhoffer T, Schilke BA, Lopez-Buesa P, Walter WA, Wiedmann M, Craig EA.
The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.
EMBO J. 1998 17(14):3981-9. DOI: 10.1093/emboj/17.14.3981. [PDF]

Baxter BK, Craig EA.
Isolation of UBP3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae.
Curr Genet. 1998 33(6):412-9. DOI: 10.1007/s002940050354. [PDF]

Kim S, Schilke B, Craig EA, Horwich AL.
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.
Proc Natl Acad Sci U S A. 1998 95(22):12860-5. DOI: 10.1073/pnas.95.22.12860. [PDF]

1997

Bergeron JJM, Craig EA, Horwich AL, Langer T, Multhoff G, Smith DF, and Hightower LE.
Molecular chaperones in biology and medicine at Obernai.
Cell Stress Chaperones. 1997 2(4): 220–228. DOI: 10.1379/1466-1268(1997)002<0220:mcibam>2.3.co;2. [PDF]

Johnson JL, Craig EA.
Protein folding in vivo: unraveling complex pathways.
Cell. 1997 90(2):201-4. DOI: 10.1016/s0092-8674(00)80327-x. [PDF]

Miao B, Davis JE, Craig EA.
Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae.
J Mol Biol. 1997 265(5):541-52. DOI: 10.1006/jmbi.1996.0762. [PDF]

Merlin A, von Ahsen O, Craig EA, Dietmeir K, Pfanner N.
A mutant form of mitochondrial GrpE suppresses the sorting defect caused by an alteration in the presequence of cytochrome b2.
J. Mol. Biol. 1997 273:1-6. DOI: 10.1006/jmbi.1997.1300. [PDF]

James P, Pfund C, Craig EA.
Functional specificity among Hsp70 molecular chaperones.
Science. 1997 275(5298):387-9. DOI: 10.1126/science.275.5298.387. [PDF]

Pfanner N, Craig EA, Honlinger A.
Mitochondrial preprotein translocase
Ann. Rev Cell Dev Biol. 1997 13:25-51. DOI: 10.1146/annurev.cellbio.13.1.25. [PDF]

Miao B, Davis J, Craig EA.
The Hsp70 family – an overview.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxfod University Press; 1997. 3-13p.

Ziegelhoffer T, Craig EA.
Saccharomyces cerevisiae Ssa proteins.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxford University Press; 1997. 26-28p.

Ziegelhoffer T, Pfund C, Craig EA.
Saccharomyces cerevisiae Ssb proteins.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxford University Press; 1997. 29-30p.

Davis J, Miao B, Craig EA.
Saccharomyces cerevisiae Ssc1.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxford University Press; 1997. 30-31p.

Craig EA.
Saccharomyces cerevisiae Ssh1p.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxford University Press; 1997. 32-33p.

Baxter B, Craig EA.
Saccharomyces cerevisiae Ssi1 protein.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding Catalysis New York, NY: Oxford University Press; 1997. 36p.

Laloraya S, Craig EA.
Saccharomyces cerevisiae Mge1.
In: Gething M-J, editor. Guidebook to Molecular Chaperones and Protein Folding CatalysisNew York, NY: Oxford University Press; 1997. 139-140p.

1996

James P, Halladay J, Craig EA.
Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast.
Genetics. 1996 144(4):1425-36. PMCID: PMC1207695 [PDF]

Baxter BK, James P, Evans T, Craig EA.
SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.
Mol Cell Biol. 1996 16(11):6444-56. DOI: 10.1128/mcb.16.11.6444. [PDF]

Becker J, Walter W, Yan W, Craig EA.
Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.
Mol Cell Biol. 1996 16(8):4378-86. DOI: 10.1128/mcb.16.8.4378. [PDF]

Schilke B, Forster J, Davis J, James P, Walter W, Laloraya S, Johnson J, Miao B, Craig E.
The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA.
J Cell Biol. 1996 134(3):603-13. DOI: 10.1083/jcb.134.3.603. [PDF]

Ziegelhoffer T, Johnson JL, Craig EA.
Protein folding: Chaperones get Hip.
Curr Biol. 1996 6(3):272-5. Review. DOI: 10.1016/s0960-9822(02)00476-1. [PDF]

1995

Laloraya S, Dekker PJ, Voos W, Craig EA, Pfanner N.
Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins.
Mol Cell Biol. 1995 15(12):7098-105. DOI: 10.1128/mcb.15.12.7098. [PDF]

Halladay JT, Craig EA.
A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant.
Mol Cell Biol. 1995 15(9):4890-7. DOI: 10.1128/mcb.15.9.4890. [PDF]

Ziegelhoffer T, Lopez-Buesa P, Craig EA.
The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates.
J Biol Chem. 1995 270(18):10412-9. DOI: 10.1074/jbc.270.18.10412. [PDF]

Hönlinger A, Keil P, Nelson RJ, Craig EA, Pfanner N.
Posttranslational mitochondrial protein import in a homologous yeast in vitro system.
Biol Chem Hoppe Seyler. 1995 376(8):515-9. PMID: 7576252 [PDF]

Gärtner F, Voos W, Querol A, Miller BR, Craig EA, Cumsky MG, Pfanner N.
Mitochondrial import of subunit Va of cytochrome c oxidase characterized with yeast mutants.
J Biol Chem. 1995 270(8):3788-95. DOI: 10.1074/jbc.270.8.3788. [PDF]

Craig E, Ziegelhoffer T, Nelson J, Laloraya S, Halladay J.
Complex multigene family of functionally distinct Hsp70s of yeast.
Cold Spring Harb Symp Quant Biol. 1995 60:441-9. DOI: 10.1101/sqb.1995.060.01.049. [PDF]

Craig EA, Ziegelhoffer T, Nelson J, Laloraya S, Halladay J.
Complex multigene family of functionally distinct hsp70s of yeast.
Cold Spring Harbor Symp. Quant. Biol., Cold Spring Harbor Press, Inc.. 1995; 60:441.

Craig EA, Gambill BD, Voos W, Pfanner N.
The role of molecular chaperones in transport of proteins across membranes.
In: Rothman S, editor. Membrane Protein Transport Greenwich, CT: JAI Press, Inc.; 1995. 1-28p. [PDF]