Genomes and Genes
Gene Symbol: SSB2
Description: Hsp70 family ATPase SSB2
Species: Saccharomyces cerevisiae S288c
- The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complexC Pfund
Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706, USA
EMBO J 17:3981-9. 1998..These interactions allow Ssb to function as a chaperone on the ribosome, preventing the misfolding of newly synthesized proteins...
- A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisVéronique Albanèse
Department of Biology, Stanford University, Palo Alto, CA 94305, USA
J Cell Biol 189:69-81. 2010..Our results demonstrate that, in addition to their known cytoplasmic roles in de novo protein folding, some ribosome-anchored CLIPS chaperones play a critical role in nuclear steps of ribosome biogenesis...
- The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkUlrike von Plehwe
Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, D 79104 Freiburg, Germany
Genes Dev 23:2102-15. 2009..The data are consistent with a model in which Ssb is crucial for efficient regulation within the SNF1 signaling network, thereby allowing an appropriate response to changing glucose levels...
- Effects of ubiquitin system alterations on the formation and loss of a yeast prionKim D Allen
School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, Georgia 30332 0230, USA
J Biol Chem 282:3004-13. 2007..We propose that UPS alterations induce an adaptive response, resulting in accumulation of the large "aggresome"-like aggregates that promote de novo prion generation and prion recovery from the chaperone treatment...
- Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 systemJoanna Bobula
Institute of Environmental Sciences, Jagiellonian University, Poland
Genetics 174:937-44. 2006..A plausible role of chaperones is to stabilize genetic networks, thus making them more tolerant to malfunctioning of their constituents...
- Specific effects of ribosome-tethered molecular chaperones on programmed -1 ribosomal frameshiftingKristi L Muldoon-Jacobs
Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA
Eukaryot Cell 5:762-70. 2006..Analysis of published DNA microarray experiments reveals conditions under which Ssb1, Ssb2, Ssz1, and Zuo1 transcript levels are regulated independently of those of genes encoding ribosomal proteins...
- Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cellsVéronique Albanèse
Department of Biological Sciences and BioX Program, Stanford University, Stanford, CA 94305, USA
Cell 124:75-88. 2006..The emergence of a translation-linked chaperone network likely underlies the elaborate cotranslational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells...
- The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and SsbLance Shaner
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030, USA
J Biol Chem 280:41262-9. 2005..These data suggest that the Hsp110 chaperone operates in concert with Hsp70 in yeast and that this collaboration is required for cellular Hsp70 functions...
- Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo foldingAlice Yen Wen Yam
Department of Biological Sciences and BioX Program, Stanford University, Stanford, California 94305 5020, USA
J Biol Chem 280:41252-61. 2005..It, thus, appears that Hsp110 is an important regulator of Hsp70-substrate interactions. Based on our data, we propose that Hsp110 cooperates with the SSB and SSA Hsp70 subfamilies, which act sequentially during de novo folding...
- Zuotin, a ribosome-associated DnaJ molecular chaperoneW Yan
Department of Biomolecular Chemistry, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA
EMBO J 17:4809-17. 1998..We propose that Zuo1 binds to ribosomes, in part, by interaction with ribosomal RNA and that Zuo1 functions with Ssb as a chaperone on the ribosome...
- Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosidesSo Young Kim
Department of Biochemistry, University of Wisconsin Madison, Madison, WI 53706, USA
Eukaryot Cell 4:82-9. 2005..We conclude that, in vivo, the major cause of the aminoglycoside sensitivity of cells lacking ribosome-associated molecular chaperones is a general increase in cation influx, perhaps due to altered maturation of membrane proteins...
- Structural snapshot of cytoplasmic pre-60S ribosomal particles bound by Nmd3, Lsg1, Tif6 and Reh1Chengying Ma
Ministry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China
Nat Struct Mol Biol . 2017..These findings pinpoint a structural checkpoint role for Nmd3 in PTC assembly, and provide information about functional and mechanistic roles of these assembly factors in the maturation of the 60S ribosomal subunit...
- Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeastJennifer L Abrams
From the Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030
J Biol Chem 289:13155-67. 2014....
- Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiaeMarco Chiabudini
Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany Center for Biological Signaling Studies BIOSS, University of Freiburg, Freiburg, Germany
Mol Cell Biol 34:4062-76. 2014..increased in the absence of the ribosome-bound chaperones ribosome-associated complex (RAC) and Ssb (Ssb1 and Ssb2)...
- Prion-Associated Toxicity is Rescued by Elimination of Cotranslational ChaperonesKathryn M Keefer
Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri, United States of America
PLoS Genet 12:e1006431. 2016..This toxicity rescue demonstrates that chaperone modification can block key steps of the prion life cycle and has exciting implications for potential treatment of many human protein conformational disorders...
- Trans-species activity of a nonself recognition domainRobert Phillip Smith
Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada
BMC Microbiol 13:63. 2013..Previous studies have shown that co-expression of the two allelic forms of un-24, Oakridge (OR) and Panama (PA), in the same cell results in cell death...
- The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasisFelix Willmund
Department of Biology and BioX Program, Stanford University, Stanford, CA 94305 5430, USA
Cell 152:196-209. 2013..Thus, cotranslationally acting Hsp70 meets the challenge of folding the eukaryotic proteome by stabilizing its longer, more slowly translated, and aggregation-prone nascent polypeptides...
- Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chainsMarco Chiabudini
Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg, Freiburg, Germany
Mol Cell Biol 32:4769-79. 2012..This active role of RAC/Ssb in the quality control of polylysine proteins significantly contributed to the low level of expression of nonstop transcripts in vivo...
- Control of the function of the transcription and repair factor TFIIH by the action of the cochaperone Ydj1María Moriel-Carretero
Centro Andaluz de Biologia Molecular y Medicina Regenerativa, Universidad de Sevilla Consejo Superior de Investigaciones Científicas, 41092 Seville, Spain
Proc Natl Acad Sci U S A 108:15300-5. 2011..Our results provide evidence for a role of chaperones in NER and transcription, with implications in cancer and TFIIH-associated syndromes...
- Insights into the role of yeast eIF2A in IRES-mediated translationLucas C Reineke
Department of Biochemistry, Case Western Reserve University, School of Medicine, Cleveland, Ohio, United States of America
PLoS ONE 6:e24492. 2011..These data suggest that eIF2A acts as a switch to regulate IRES-mediated translation, and eEF1A may be an important mediator of translational activation during ethanol stress...
- GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3 proteinLidija Staresincic
Mechanisms of Transcription Laboratory, Clare Hall Laboratories, Cancer Research UK London Research Institute, South Mimms EN6 3LD, UK
J Biol Chem 286:35553-61. 2011..Together, our data suggest that Npa3 defines an unconventional pathway for nuclear import of RNAPII, which involves GTP-dependent binding of Npa3 to the polymerase...
- Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiensSimona Panni
Department of Biology, University of Rome Tor Vergata, Rome, Italy
Proteomics 11:128-43. 2011..Our approach provides an orthogonal reliability assessment and maps with high confidence the 14-3-3 peptide target on the partner proteins...
- Characterizing the connectivity of poly-ubiquitin chains by selected reaction monitoring mass spectrometryHamid Mirzaei
Institute for Systems Biology, Seattle, WA 98103, USA
Mol Biosyst 6:2004-14. 2010..cerevisiae. We then applied the method to detect toxin induced changes in the poly-ubiquitination profile in complex and enriched protein samples...
- Metacaspase Yca1 is required for clearance of insoluble protein aggregatesRobin E C Lee
Ottawa Hospital Research Institute, Sprott Centre for Stem Cell Research, Ottawa Hospital, and Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON, Canada K1H 8L6
Proc Natl Acad Sci U S A 107:13348-53. 2010..Together, our results show that Yca1 contributes to the fitness and adaptability of growing yeast through an aggregate remodeling activity...
- The translation machinery and 70 kd heat shock protein cooperate in protein synthesisR J Nelson
Department of Biomolecular Chemistry, University of Wisconsin Madison 53706
Cell 71:97-105. 1992..Mutant ssb1 ssb2 strains grow slowly, contain a low number of translating ribosomes, and are hypersensitive to several inhibitors of ..
- A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomesAnsgar Koplin
Laboratory of Molecular Microbiology, Department of Biology, and 2 Konstanz Research School of Chemical Biology, University of Konstanz, 78457 Konstanz, Germany
J Cell Biol 189:57-68. 2010..These findings emphasize the concept that ribosome production is coordinated with the protein-folding capacity of ribosome-associated chaperones...
- Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone systemAtin K Mandal
Department of Biology, The City College of New York, New York, NY 10031, USA
Mol Biol Cell 21:1439-48. 2010..These findings support a model in which Hsp110 chaperones contribute significantly to the decision made by Hsp70 to fold or degrade a client protein...
- Yeast Uri1p promotes translation initiation and may provide a link to cotranslational quality controlAnna Deplazes
Department of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland or
EMBO J 28:1429-41. 2009..Together with genetic data, these interactions indicate that Uri1p may coordinate translation initiation and cotranslational quality control...
- Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partnersT Michimoto
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7 3 1 Hongo, Tokyo 113 0033, Bunkyo ku, Japan
Gene 257:131-7. 2000..Taken together, we propose that Pdr13p and Zuo1p are a new pair of Hsp70:Hsp40 molecular chaperones. In addition, Pdr13p co-sedimented with translating ribosomes and this association was independent of the presence of Zuo1p...
- The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiaeKenneth M Dombek
Department of Biochemistry, University of Washington, Seattle, Washington 98195 7350, USA
J Biol Chem 279:39165-74. 2004..Here we show that the Reg1-interacting proteins Bmh1, Bmh2, Ssb1, and Ssb2 have roles in glucose repression...
- The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiaeMagdalena Rakwalska
Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Hermann Herder Strasse 7, D 79104 Freiburg, Germany
Mol Cell Biol 24:9186-97. 2004..Based on the combined data we conclude that RAC and Ssb1/2p are crucial in maintaining translational fidelity beyond their postulated role as chaperones for nascent polypeptides...
- The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeresHaiying Zhang
Department of Oncological Sciences, School of Medicine, University of Utah, 2000 Circle of Hope, Salt Lake City, UT 84112, USA
Mol Cell Biol 24:9424-36. 2004..Taken together, these data indicate that Yaf9 may function in NuA4 and SWR1 complexes to help antagonize silencing near telomeres...
- Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiaeKarin Elbing
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA
Biochem J 393:797-805. 2006..Finally, we showed that the Snf1 kinase domain isolated from bacteria as a GST fusion protein can be activated in vitro and shows substrate specificity in the absence of its beta and gamma subunits...
- Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complexDavid Li En Jao
Department of Chemistry and Chemical Biology, Rutgers The State University of New Jersey, Piscataway, NJ 08854 8087, USA
J Cell Biochem 97:583-98. 2006....
- Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiaeY Kosodo
Department of Biotechnology, University of Tokyo, Yayoi, Bunkyo ku, Tokyo 113 8657, Japan
Yeast 18:1003-14. 2001..were classified as: (1) those that encode a multifunctional suppressor, SSD1; (2) heat shock proteins, SSB1 and SSB2; (3) cell surface proteins, WSC1, WSC2 and MID2; (4) ER-Golgi transport proteins, USO1 and BET1; and (5) an as-yet-..
- A novel multiple affinity purification tag and its use in identification of proteins associated with a cyclin-CDK complexS Honey
Cold Spring Harbor Laboratories, Cold Spring Harbor, NY 11724, USA
Nucleic Acids Res 29:E24. 2001..Associated proteins were identified using mass spectrometry. These included the known associated proteins Cdc28, Sic1 and Cks1. Several other proteins were found including the 70 kDa chaperone, Ssa1...
- The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptidesMatthias Gautschi
Max Planck Research Unit Enzymology of Protein Folding, D 06120 Halle, Germany
Mol Cell Biol 23:7403-14. 2003..The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis...
- Complex regulation of the yeast heat shock transcription factorJ J Bonner
Department of Biology, Indiana University, Bloomington, Indiana 47405 3700, USA
Mol Biol Cell 11:1739-51. 2000....
- Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1pZdravko Dragovic
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
Biol Chem 387:1593-600. 2006..Interestingly, Fes1p inhibits the stimulation of Ssb1p ATPase by RAC, suggesting a complex regulatory role of Fes1p in modulating the function of Ssb Hsp70s in co-translational protein folding...
- The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domainsP Lopez-Buesa
Department of Biomolecular Chemistry, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA
Proc Natl Acad Sci U S A 95:15253-8. 1998..The differential influence of the peptide-binding domain on the ATPase domain may, in part, explain the functional uniqueness of these two classes of Hsp70s...
- Identification of the divergent calmodulin binding motif in yeast Ssb1/Hsp75 protein and in other HSP70 family membersR C Heinen
Departamento de Bioquimica, Instituto de Quimica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil
Braz J Med Biol Res 39:1399-408. 2006..A model in which calmodulin displaces Bag-1 and modulates Ssb1/Hsp75 chaperone activity is discussed...
- A role for the yeast cell cycle/splicing factor Cdc40 in the G1/S transitionYosef Kaplan
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, 69978, Israel
Curr Genet 51:123-40. 2007..Finally, we discuss possible mechanisms of suppression by the cDNAs that imply cell cycle regulation by apparently unrelated processes, such as splicing, translation initiation and glycolysis...
- Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complexCharlotte Conz
Institute of Biochemistry and Molecular Biology, Zentrum für Biochemie und Molekulare Zellforschung ZBMZ, University of Freiburg, Herrmann Herder Strasse 7, Freiburg, Germany
J Biol Chem 282:33977-84. 2007..The two domains of this protein thus cooperate in a way that allows for severe interference in either but not in both of them...
- Alleviation of deleterious effects of protein mutation through inactivation of molecular chaperonesKatarzyna Tomala
Institute of Environmental Sciences, Jagiellonian University, Gronostajowa 7, 30 387, Krakow, Poland
Mol Genet Genomics 280:409-17. 2008..We suggest that under non-stressful conditions, molecular chaperones are tuned to support folding of native proteins, but not that of mutated ones...
- TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classesKatja Siegers
Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, D 82152 Martinsried, Germany
EMBO J 22:5230-40. 2003..These findings expand the substrate range of the eukaryotic chaperonin by a structurally defined class of proteins and demonstrate an essential role for upstream chaperones in TRiC-assisted folding...
- POSTTRANSLATIONAL REGULATION OF HSF ACTIVITYJames Bonner; Fiscal Year: 2002..These will identify those cellular systems that require HSF activity in the absence of stress, and thus reveal why HSF is an essential gene in yeast. ..