Literature DB >> 18389627

[Transcription factor YY1 participates in activation transcription of the human ribosomal protein L11 gene].

E N Voronina, T D Kolokol'tsova, N M Slyn'ko, E A Nechaev, M L Filipenko.   

Abstract

Ribosomal protein L11 plays important role in ribosome, being involved in several steps in protein synthesis and also activates p53-dependent cell cycle arrest. Changes in the rpL11 levels might be implicated in cell cycle control and carcinogenesis. Therefore, the mechanism of regulation of rpL11 expression has increasing importance. Article presents research results of interaction of promotor elements of gene HRPL11 with proteins of nuclear extracts of cells of a various cell origin. Use oligonucleotide competitors containing known transcription factor-binding sites, and also polyclonal antibodies has shown, that transcription factor YY1 participates in regulation of a transcription of gene HRPL11 in all investigated cellular lines. Our data obtained from comparison of protein binding profiles using nuclear extracts from rapidly growth cells, normal cell lines and serum deprivation repressed cell allows us to consider of transcription factor YY1 as activator of HRPL11 gene transcription.

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Year:  2008        PMID: 18389627     DOI: 10.1134/s0026893308010160

Source DB:  PubMed          Journal:  Mol Biol (Mosk)        ISSN: 0026-8984


  27 in total

1.  Oligopeptide-repeat expansions modulate 'protein-only' inheritance in yeast.

Authors:  J J Liu; S Lindquist
Journal:  Nature       Date:  1999-08-05       Impact factor: 49.962

Review 2.  Shattuck lecture--neurodegenerative diseases and prions.

Authors:  S B Prusiner
Journal:  N Engl J Med       Date:  2001-05-17       Impact factor: 91.245

3.  Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Authors:  J R Glover; S Lindquist
Journal:  Cell       Date:  1998-07-10       Impact factor: 41.582

Review 4.  HSP100/Clp proteins: a common mechanism explains diverse functions.

Authors:  E C Schirmer; J R Glover; M A Singer; S Lindquist
Journal:  Trends Biochem Sci       Date:  1996-08       Impact factor: 13.807

5.  Chaperone-supervised conversion of prion protein to its protease-resistant form.

Authors:  S K DebBurman; G J Raymond; B Caughey; S Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  1997-12-09       Impact factor: 11.205

6.  Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP.

Authors:  E C Schirmer; S Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  1997-12-09       Impact factor: 11.205

7.  The 5'-leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo.

Authors:  D R Gallie; D E Sleat; J W Watts; P C Turner; T M Wilson
Journal:  Nucleic Acids Res       Date:  1987-04-24       Impact factor: 16.971

Review 8.  The molecular chaperone Hsp104--a molecular machine for protein disaggregation.

Authors:  Benjamin Bösl; Valerie Grimminger; Stefan Walter
Journal:  J Struct Biol       Date:  2006-03-06       Impact factor: 2.867

9.  Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae.

Authors:  I L Derkatch; M E Bradley; P Zhou; Y O Chernoff; S W Liebman
Journal:  Genetics       Date:  1997-10       Impact factor: 4.562

10.  Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.

Authors:  D A Parsell; Y Sanchez; J D Stitzel; S Lindquist
Journal:  Nature       Date:  1991-09-19       Impact factor: 49.962

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