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

Detalhes bibliográficos
Autor(a) principal: Correia,Heriberto
Data de Publicação: 2004
Outros Autores: Medina,Rafael, Hernández,Alexandra, Bustamante,Ekaterina, Chakraburtty,Kalpana, Herrera,Flor
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762004000700012
Resumo: 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.
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spelling Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiaeribosomal association factorStm1pG4 DNAribosomal functionG4p2triplex-DNAA 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.Instituto Oswaldo Cruz, Ministério da Saúde2004-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762004000700012Memórias do Instituto Oswaldo Cruz v.99 n.7 2004reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762004000700012info:eu-repo/semantics/openAccessCorreia,HeribertoMedina,RafaelHernández,AlexandraBustamante,EkaterinaChakraburtty,KalpanaHerrera,Floreng2020-04-25T17:49:18Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:12:49.047Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
title Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
spellingShingle Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
Correia,Heriberto
ribosomal association factor
Stm1p
G4 DNA
ribosomal function
G4p2
triplex-DNA
title_short Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
title_full Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
title_fullStr Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
title_full_unstemmed Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
title_sort Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae
author Correia,Heriberto
author_facet Correia,Heriberto
Medina,Rafael
Hernández,Alexandra
Bustamante,Ekaterina
Chakraburtty,Kalpana
Herrera,Flor
author_role author
author2 Medina,Rafael
Hernández,Alexandra
Bustamante,Ekaterina
Chakraburtty,Kalpana
Herrera,Flor
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Correia,Heriberto
Medina,Rafael
Hernández,Alexandra
Bustamante,Ekaterina
Chakraburtty,Kalpana
Herrera,Flor
dc.subject.por.fl_str_mv ribosomal association factor
Stm1p
G4 DNA
ribosomal function
G4p2
triplex-DNA
topic ribosomal association factor
Stm1p
G4 DNA
ribosomal function
G4p2
triplex-DNA
dc.description.none.fl_txt_mv 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.
description 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.
publishDate 2004
dc.date.none.fl_str_mv 2004-11-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762004000700012
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762004000700012
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762004000700012
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.99 n.7 2004
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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