A glutamine/asparagine-rich fragment of Gln3, but not the full-length protein, aggregates in Saccharomyces cerevisiae

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• 作者：K. S. Antonets ; H. M. Sargsyan ; A. A. Nizhnikov
• 刊名：Biochemistry (Moscow)
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：81
• 期：4
• 页码：407-413
• 全文大小：444 KB
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040
• 卷排序：81

文摘

The amino acid sequence of protein Gln3 in yeast Saccharomyces cerevisiae has a region enriched with Gln (Q) and Asn (N) residues. In this study, we analyzed the effects of overexpression of Gln3 and its Q/N-rich fragment fused with yellow fluorescent protein (YFP). Being overexpressed, full-length Gln3-YFP does not form aggregates, inhibits vegetative growth, and demonstrates nuclear localization, while the Q/N-rich fragment (Gln3QN) fused with YFP forms aggregates that do not colocalize with the nucleus and do not affect growth of the cells. Although detergent-resistant aggregates of Gln3QN are formed in the absence of yeast prions, the aggregation of Gln3QN significantly increases in the presence of [PIN+] prion, while in the presence of two prions, [PSI+] and [PIN+], the percentage of cells with Gln3QN aggregates is significantly lower than in the strain bearing only [PIN+]. Data on colocalization demonstrate that this effect is mediated by interaction between Gln3QN aggregates and [PSI+] and [PIN+] prions.KeywordsamyloidprionGln3Rnq1Sup35yeastS. cerevisiae