schliessen

Filtern

 

Bibliotheken

Mutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis

Myogenin is a muscle-specific nuclear factor that acts as a genetic switch to activate myogenesis. Myogenin, MyoD, and a growing number of proteins implicated in transcriptional control share sequence homology within a basic region and an adjacent helix-loop-helix motif. Here we identify by site-dir... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 01 July 1991, Vol.88(13), p.5675
Main Author: T J Brennan
Other Authors: T Chakraborty , E N Olson
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424 ; E-ISSN: 1091-6490
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: pnas_s88_13_5675
title: Mutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis
format: Article
creator:
  • T J Brennan
  • T Chakraborty
  • E N Olson
subjects:
  • Sciences (General)
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 01 July 1991, Vol.88(13), p.5675
description: Myogenin is a muscle-specific nuclear factor that acts as a genetic switch to activate myogenesis. Myogenin, MyoD, and a growing number of proteins implicated in transcriptional control share sequence homology within a basic region and an adjacent helix-loop-helix motif. Here we identify by site-directed mutagenesis a 12-amino acid subdomain of the myogenin basic region essential for binding of DNA and activation of myogenesis. The basic region of the widely expressed helix-loop-helix protein E12 is conserved at 8 of these 12 residues and can mediate DNA binding when placed in myogenin, but it cannot activate myogenesis. Replacement of each of the four nonconserved residues of the myogenin basic region with the corresponding residues of E12 reveals two adjacent amino acids (Ala86-Thr) that can impart muscle specificity to the basic region. These residues are specific to, and conserved in, the basic regions of all known myogenic helix-loop-helix proteins from Drosophila to man, suggesting that they constitute part of an ancient protein motif required for activation of the myogenic program.
language: eng
source:
identifier: ISSN: 0027-8424 ; E-ISSN: 1091-6490
fulltext: fulltext_linktorsrc
issn:
  • 0027-8424
  • 00278424
  • 1091-6490
  • 10916490
url: Link


@attributes
ID1300649137
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid88_13_5675
sourceidpnas_s
recordidTN_pnas_s88_13_5675
sourcesystemPC
dbid
0PNE
1RNA
pqid80651824
display
typearticle
titleMutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis
creatorT J Brennan ; T Chakraborty ; E N Olson
ispartofProceedings of the National Academy of Sciences of the United States of America, 01 July 1991, Vol.88(13), p.5675
identifierISSN: 0027-8424 ; E-ISSN: 1091-6490
subjectSciences (General)
descriptionMyogenin is a muscle-specific nuclear factor that acts as a genetic switch to activate myogenesis. Myogenin, MyoD, and a growing number of proteins implicated in transcriptional control share sequence homology within a basic region and an adjacent helix-loop-helix motif. Here we identify by site-directed mutagenesis a 12-amino acid subdomain of the myogenin basic region essential for binding of DNA and activation of myogenesis. The basic region of the widely expressed helix-loop-helix protein E12 is conserved at 8 of these 12 residues and can mediate DNA binding when placed in myogenin, but it cannot activate myogenesis. Replacement of each of the four nonconserved residues of the myogenin basic region with the corresponding residues of E12 reveals two adjacent amino acids (Ala86-Thr) that can impart muscle specificity to the basic region. These residues are specific to, and conserved in, the basic regions of all known myogenic helix-loop-helix proteins from Drosophila to man, suggesting that they constitute part of an ancient protein motif required for activation of the myogenic program.
languageeng
source
version7
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
linktorsrc$$Uhttp://www.pnas.org/content/88/13/5675.abstract$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
search
creatorcontrib
0T J Brennan
1T Chakraborty
2E N Olson
titleMutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis
description

Myogenin is a muscle-specific nuclear factor that acts as a genetic switch to activate myogenesis. Myogenin, MyoD, and a growing number of proteins implicated in transcriptional control share sequence homology within a basic region and an adjacent helix-loop-helix motif. Here we identify by site-directed mutagenesis a 12-amino acid subdomain of the myogenin basic region essential for binding of DNA and activation of myogenesis. The basic region of the widely expressed helix-loop-helix protein E12 is conserved at 8 of these 12 residues and can mediate DNA binding when placed in myogenin, but it cannot activate myogenesis. Replacement of each of the four nonconserved residues of the myogenin basic region with the corresponding residues of E12 reveals two adjacent amino acids (Ala86-Thr) that can impart muscle specificity to the basic region. These residues are specific to, and conserved in, the basic regions of all known myogenic helix-loop-helix proteins from Drosophila to man, suggesting that they constitute part of an ancient protein motif required for activation of the myogenic program.

subjectSciences (General)
general
0English
1National Acad Sciences
2PNAS (National Academy of Sciences)
3National Academy of Sciences (U.S.)
sourceidpnas_s
recordidpnas_s88_13_5675
issn
00027-8424
100278424
21091-6490
310916490
rsrctypearticle
creationdate1991
addtitleProceedings of the National Academy of Sciences of the United States of America
searchscope
0pnas_full
1pnas4
2pnas5
scope
0pnas_full
1pnas4
2pnas5
lsr45$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
tmp01
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
tmp02
0PNE
1RNA
startdate19910701
enddate19910701
lsr40Proceedings of the National Academy of Sciences of the United States of America, 01 July 1991, Vol.88 (13), p.5675
citationpf 5675 vol 88 issue 13
lsr30VSR-Enriched:[doi, pqid, pages]
sort
titleMutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis
authorT J Brennan ; T Chakraborty ; E N Olson
creationdate19910701
lso0119910701
facets
frbrgroupid6464750885352668045
frbrtype5
newrecords20190724
languageeng
topicSciences (General)
collection
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
prefilterarticles
rsrctypearticles
creatorcontrib
0T J Brennan
1T Chakraborty
2E N Olson
jtitleProceedings of the National Academy of Sciences of the United States of America
creationdate1991
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext_linktorsrc
addata
au
0T J Brennan
1T Chakraborty
2E N Olson
atitleMutagenesis of the myogenin basic region identifies an ancient protein motif critical for activation of myogenesis
jtitleProceedings of the National Academy of Sciences of the United States of America
risdate19910701
volume88
issue13
spage5675
issn0027-8424
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
abstract

Myogenin is a muscle-specific nuclear factor that acts as a genetic switch to activate myogenesis. Myogenin, MyoD, and a growing number of proteins implicated in transcriptional control share sequence homology within a basic region and an adjacent helix-loop-helix motif. Here we identify by site-directed mutagenesis a 12-amino acid subdomain of the myogenin basic region essential for binding of DNA and activation of myogenesis. The basic region of the widely expressed helix-loop-helix protein E12 is conserved at 8 of these 12 residues and can mediate DNA binding when placed in myogenin, but it cannot activate myogenesis. Replacement of each of the four nonconserved residues of the myogenin basic region with the corresponding residues of E12 reveals two adjacent amino acids (Ala86-Thr) that can impart muscle specificity to the basic region. These residues are specific to, and conserved in, the basic regions of all known myogenic helix-loop-helix proteins from Drosophila to man, suggesting that they constitute part of an ancient protein motif required for activation of the myogenic program.

pubNational Acad Sciences
urlhttp://www.pnas.org/content/88/13/5675.abstract
lad01Proceedings of the National Academy of Sciences of the United States of America
doi10.1073/pnas.88.13.5675
pages5675-5679
date1991-07-01