Research output: Contribution to journal › Article › peer-review
To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1. / Barbitoff, Yury A.; Matveenko, Andrew G.; Moskalenko, Svetlana E.; Zemlyanko, Olga M.; Newnam, Gary P.; Patel, Ayesha; Chernova, Tatiana A.; Chernoff, Yury O.; Zhouravleva, Galina A.
In: Molecular Microbiology, Vol. 105, No. 2, 07.2017, p. 242-257.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1
AU - Barbitoff, Yury A.
AU - Matveenko, Andrew G.
AU - Moskalenko, Svetlana E.
AU - Zemlyanko, Olga M.
AU - Newnam, Gary P.
AU - Patel, Ayesha
AU - Chernova, Tatiana A.
AU - Chernoff, Yury O.
AU - Zhouravleva, Galina A.
PY - 2017/7
Y1 - 2017/7
N2 - Yeast self-perpetuating protein aggregates (prions) provide a convenient model for studying various components of the cellular protein quality control system. Molecular chaperones and chaperone-sorting factors, such as yeast Cur1 protein, play key role in proteostasis via tight control of partitioning and recycling of misfolded proteins. In this study, we show that, despite the previously described ability of Cur1 to antagonize the yeast prion [URE3], it enhances propagation and phenotypic manifestation of another prion, [PSI+]. We demonstrate that both curing of [URE3] and enhancement of [PSI+] in the presence of excess Cur1 are counteracted by the cochaperone Hsp40-Sis1 in a dosage-dependent manner, and show that the effect of Cur1 on prions parallels effects of the attachment of nuclear localization signal to Sis1, indicating that Cur1 acts on prions via its previously reported ability to relocalize Sis1 from the cytoplasm to nucleus. This shows that the direction in which Cur1 influences a prion depends on how this specific prion responds to relocalization of Sis1.
AB - Yeast self-perpetuating protein aggregates (prions) provide a convenient model for studying various components of the cellular protein quality control system. Molecular chaperones and chaperone-sorting factors, such as yeast Cur1 protein, play key role in proteostasis via tight control of partitioning and recycling of misfolded proteins. In this study, we show that, despite the previously described ability of Cur1 to antagonize the yeast prion [URE3], it enhances propagation and phenotypic manifestation of another prion, [PSI+]. We demonstrate that both curing of [URE3] and enhancement of [PSI+] in the presence of excess Cur1 are counteracted by the cochaperone Hsp40-Sis1 in a dosage-dependent manner, and show that the effect of Cur1 on prions parallels effects of the attachment of nuclear localization signal to Sis1, indicating that Cur1 acts on prions via its previously reported ability to relocalize Sis1 from the cytoplasm to nucleus. This shows that the direction in which Cur1 influences a prion depends on how this specific prion responds to relocalization of Sis1.
KW - DISEASE-RELATED PROTEIN
KW - RELEASE FACTORS ERF1
KW - SACCHAROMYCES-CEREVISIAE
KW - URE3 PRION
KW - TRANSLATION TERMINATION
KW - ANTAGONISTIC INTERACTIONS
KW - MOLECULAR CHAPERONES
KW - DEPENDENT LETHALITY
KW - SHUTTLE VECTORS
KW - IMAGE-ANALYSIS
UR - http://www.scopus.com/inward/record.url?scp=85019034618&partnerID=8YFLogxK
U2 - 10.1111/mmi.13697
DO - 10.1111/mmi.13697
M3 - статья
AN - SCOPUS:85019034618
VL - 105
SP - 242
EP - 257
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 2
ER -
ID: 9131506