Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog Journal Article

   


Authors: Garrett, K. P.; Aso, T.; Bradsher, J. N.; Foundling, S. I.; Lane, W. S.; Conaway, R. C.; Conaway, J. W.
Article Title: Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
Abstract: General transcription factor SIII, a heterotrimer composed of 110-kDa (p110), 18-kDa (p18), and 15-kDa (p15) subunits, increases the catalytic rate of transcribing RNA polymerase II by suppressing transient pausing by polymerase at multiple sites on DNA templates. Here we report molecular cloning and biochemical characterization of the SIII p18 subunit, which is found to be a member of the ubiquitin homology (UbH) gene family and functions as a positive regulatory subunit of SIII. p18 is a 118-amino acid protein composed of an 84-residue N-terminal UbH domain fused to a 34- residue C-terminal tail. Mechanistic studies indicate that p18 activates SIII transcriptional activity above a basal level inherent in the SIII p110 and p15 subunits. Taken together, these findings establish a role for p18 in regulating the activity of the RNA polymerase II elongation complex, and they bring to light a function for a UbH domain protein in transcriptional regulation.
Keywords: ubiquitin; binding affinity; protein conformation; animal; carboxy terminal sequence; transcription factor; genetic transcription; enzyme activity; transcription factors; molecular cloning; cloning, molecular; amino acid sequence; molecular sequence data; sequence homology, amino acid; amino terminal sequence; rna synthesis; base sequence; models, molecular; rats; catalysis; molecular weight; rna polymerase ii; in vitro; multigene family; dna, complementary; ubiquitins; dna template; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 92
Issue: 16
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1995-08-01
Start Page: 7172
End Page: 7176
Language: English
DOI: 10.1073/pnas.92.16.7172
PUBMED: 7638163
PROVIDER: scopus
PMCID: PMC41301
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029144904&doi=10.1073%2fpnas.92.16.7172&partnerID=40&md5=9912d9b459f28447d1f910ef025d6435
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
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