Document Detail


The polymyositis-scleroderma autoantigen interacts with the helix-loop-helix proteins E12 and E47.
MedLine Citation:
PMID:  9148967     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The basic helix-loop-helix (bHLH) transcription factors E12 and E47 regulate cellular differentiation and proliferation in diverse cell types. While looking for proteins that bind to E12 and E47 by the yeast interaction trap, we isolated the rat (r) homologue of the human (h) polymyositis-scleroderma autoantigen (PM-Scl), which has been localized to the granular layer of the nucleolus and to distinct nucleocytoplasmic foci. The rPM-Scl and hPM-Scl homologues are 96% similar and 91% identical. We found that rPM-Scl mRNA expression was regulated by growth factor stimulation in cultured rat aortic smooth muscle cells. rPM-Scl bound to E12 and E47 but not to Id3, Gax, Myb, OCT-1, or Max. The C terminus of rPM-Scl (amino acids 283-353) interacted specifically with a 54-amino acid domain in E12 that is distinct from the bHLH domain. Finally, cotransfection of rPM-Scl and E47 specifically increased the promoter activity of a luciferase reporter construct containing an E box and did not affect the basal activity of the reporter construct. rPM-Scl appears to be a novel non-HLH-interacting partner of E12/E47 that regulates E2A protein transcription.
Authors:
C J Kho; G S Huggins; W O Endege; C Patterson; M K Jain; M E Lee; E Haber
Related Documents :
15534927 - Effects of c-myb antisense rna on tgf-beta1 and beta1-i collagen expression in cultured...
10022807 - Phenotypic analysis of human glioma cells expressing the mmac1 tumor suppressor phospha...
9148967 - The polymyositis-scleroderma autoantigen interacts with the helix-loop-helix proteins e...
24927407 - Distribution and levels of cell surface expression of cd33 and cd123 in acute myeloid l...
21956967 - Alternative mrna polyadenylation in eukaryotes: an effective regulator of gene expression.
20385167 - Vitamin d does not modulate nf-kappab activity in jurkat t cells.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  272     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1997 May 
Date Detail:
Created Date:  1997-06-19     Completed Date:  1997-06-19     Revised Date:  2011-12-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13426-31     Citation Subset:  IM    
Affiliation:
Cardiovascular Biology Laboratory, Harvard School of Public Health, Boston, Massachusetts 02115, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Aorta / metabolism
Autoantigens / genetics,  metabolism*
Cells, Cultured
DNA, Complementary / genetics
DNA-Binding Proteins / genetics,  metabolism*
Exoribonucleases
Gene Expression Regulation*
Helix-Loop-Helix Motifs / genetics
Humans
Molecular Sequence Data
Muscle, Smooth, Vascular / metabolism*
Nuclear Proteins / genetics,  metabolism*
RNA, Messenger / genetics*
Rats
TCF Transcription Factors
Transcription Factor 7-Like 1 Protein
Transcription Factors / genetics,  metabolism
Transcription, Genetic
Grant Support
ID/Acronym/Agency:
R01GM 53249/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Autoantigens; 0/DNA, Complementary; 0/DNA-Binding Proteins; 0/Nuclear Proteins; 0/RNA, Messenger; 0/TCF Transcription Factors; 0/TCF7L1 protein, human; 0/Tcf7l1 protein, rat; 0/Transcription Factor 7-Like 1 Protein; 0/Transcription Factors; EC 3.1.-/Exoribonucleases; EC 3.1.13.-/EXOSC10 protein, human

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines...
Next Document:  A sequential two-step mechanism for the production of the mature p17:p12 form of caspase-3 in vitro.