Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae.

Abstract:

:A ribosome association factor (AF) was isolated from the yeast Sacchharomyces cerevisiae. Partial amino acid sequence of AF was determined from its fragment of 25 kDa isolated by treating AF with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-Bromoindolenine (BNPS-skatole). This sequence has a 86% identity to the product of the single-copy S. cerevisiae STM1 gene that is apparently involved in several events like binding to quadruplex and triplex nucleic acids and participating in apoptosis, stability of telomere structures, cell cycle, and ribosomal function. Here we show that AF and Stm1p share some characteristics: both bind to quadruplex and Pu triplex DNA, associates ribosomal subunits, and are thermostable. These observations suggest that these polypeptides belong to a family of proteins that may have roles in the translation process.

journal_name

Mem Inst Oswaldo Cruz

authors

Correia H,Medina R,Hernández A,Bustamante E,Chakraburtty K,Herrera F

doi

10.1590/s0074-02762004000700012

subject

Has Abstract

pub_date

2004-11-01 00:00:00

pages

733-7

issue

7

eissn

0074-0276

issn

1678-8060

pii

S0074-02762004000700012

journal_volume

99

pub_type

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