Standard

Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level. / Rubel', A. A.; Saǐfitdinova, A. F.; Lada, A. G.; Nizhnikov, A. A.; Inge-Vechtomov, S. G.; Galkin, A. P.

в: Molekuliarnaia biologiia, Том 42, № 1, 01.01.2008, стр. 123-130.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Rubel', AA, Saǐfitdinova, AF, Lada, AG, Nizhnikov, AA, Inge-Vechtomov, SG & Galkin, AP 2008, 'Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level', Molekuliarnaia biologiia, Том. 42, № 1, стр. 123-130.

APA

Rubel', A. A., Saǐfitdinova, A. F., Lada, A. G., Nizhnikov, A. A., Inge-Vechtomov, S. G., & Galkin, A. P. (2008). Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level. Molekuliarnaia biologiia, 42(1), 123-130.

Vancouver

Rubel' AA, Saǐfitdinova AF, Lada AG, Nizhnikov AA, Inge-Vechtomov SG, Galkin AP. Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level. Molekuliarnaia biologiia. 2008 Янв. 1;42(1):123-130.

Author

Rubel', A. A. ; Saǐfitdinova, A. F. ; Lada, A. G. ; Nizhnikov, A. A. ; Inge-Vechtomov, S. G. ; Galkin, A. P. / Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level. в: Molekuliarnaia biologiia. 2008 ; Том 42, № 1. стр. 123-130.

BibTeX

@article{cd4b9b4736f343adb03f98b77f667d51,
title = "Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level",
abstract = "Yeast chaperon Hsp104 is known as a protein which is able to dissociate aggregates of the heat damaged proteins and prion aggregates into smaller pieces or monomers. In our work the effects of Hsp104 on the PrP-GFP and GFP proteins have been analyzed. The PrP-GFP protein forms the high molecular weight aggregates, whereas GFP is unable to aggregate in yeast cell. We have shown that Hsp104 regulates the amount of PrP-GFP and GFP in yeast cells and direction of chaperone action depends on promoter controlling production of these proteins. The overproduction of Hsp104 increases the amount of PrP-GFP and GFP proteins when the corresponding genes are under control of CUP1 promoter. In contrast, the overproduction of Hsp104 decreases the amount of PrP-GFP and GFP is case of their expression under control of GPD promoter. The effects of Hspl04 are not related with any changes in mRNA content of the genes under investigation and with ability of the proteins to form aggregates. Thus, the functions of this chaperon are not restricted by dissociation of the protein aggregates. Our data show that Hsp104 regulates the gene expression on the posttranscriptional level.",
author = "Rubel', {A. A.} and Saǐfitdinova, {A. F.} and Lada, {A. G.} and Nizhnikov, {A. A.} and Inge-Vechtomov, {S. G.} and Galkin, {A. P.}",
year = "2008",
month = jan,
day = "1",
language = "English",
volume = "42",
pages = "123--130",
journal = "МОЛЕКУЛЯРНАЯ БИОЛОГИЯ",
issn = "0026-8984",
publisher = "Российская академия наук",
number = "1",

}

RIS

TY - JOUR

T1 - Yeast chaperone Hspl04 regulates gene expression on the posttranscriptional level

AU - Rubel', A. A.

AU - Saǐfitdinova, A. F.

AU - Lada, A. G.

AU - Nizhnikov, A. A.

AU - Inge-Vechtomov, S. G.

AU - Galkin, A. P.

PY - 2008/1/1

Y1 - 2008/1/1

N2 - Yeast chaperon Hsp104 is known as a protein which is able to dissociate aggregates of the heat damaged proteins and prion aggregates into smaller pieces or monomers. In our work the effects of Hsp104 on the PrP-GFP and GFP proteins have been analyzed. The PrP-GFP protein forms the high molecular weight aggregates, whereas GFP is unable to aggregate in yeast cell. We have shown that Hsp104 regulates the amount of PrP-GFP and GFP in yeast cells and direction of chaperone action depends on promoter controlling production of these proteins. The overproduction of Hsp104 increases the amount of PrP-GFP and GFP proteins when the corresponding genes are under control of CUP1 promoter. In contrast, the overproduction of Hsp104 decreases the amount of PrP-GFP and GFP is case of their expression under control of GPD promoter. The effects of Hspl04 are not related with any changes in mRNA content of the genes under investigation and with ability of the proteins to form aggregates. Thus, the functions of this chaperon are not restricted by dissociation of the protein aggregates. Our data show that Hsp104 regulates the gene expression on the posttranscriptional level.

AB - Yeast chaperon Hsp104 is known as a protein which is able to dissociate aggregates of the heat damaged proteins and prion aggregates into smaller pieces or monomers. In our work the effects of Hsp104 on the PrP-GFP and GFP proteins have been analyzed. The PrP-GFP protein forms the high molecular weight aggregates, whereas GFP is unable to aggregate in yeast cell. We have shown that Hsp104 regulates the amount of PrP-GFP and GFP in yeast cells and direction of chaperone action depends on promoter controlling production of these proteins. The overproduction of Hsp104 increases the amount of PrP-GFP and GFP proteins when the corresponding genes are under control of CUP1 promoter. In contrast, the overproduction of Hsp104 decreases the amount of PrP-GFP and GFP is case of their expression under control of GPD promoter. The effects of Hspl04 are not related with any changes in mRNA content of the genes under investigation and with ability of the proteins to form aggregates. Thus, the functions of this chaperon are not restricted by dissociation of the protein aggregates. Our data show that Hsp104 regulates the gene expression on the posttranscriptional level.

UR - http://www.scopus.com/inward/record.url?scp=43849093511&partnerID=8YFLogxK

M3 - Article

C2 - 18389629

AN - SCOPUS:43849093511

VL - 42

SP - 123

EP - 130

JO - МОЛЕКУЛЯРНАЯ БИОЛОГИЯ

JF - МОЛЕКУЛЯРНАЯ БИОЛОГИЯ

SN - 0026-8984

IS - 1

ER -

ID: 35907514