Baculovirus-expressed myogenic determination factors require E12 complex formation for binding to the myosin-light-chain enhancer

T. Braun, K. Gearing, W. E. Wright, H. H. Arnold

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Two recombinant baculoviruses BcV-myf4 and BcV-myf5 have been constructed to synthesize the human myogenic determination factors myogenin (myf4) and myf5 in eucaryotic cells. Both recombinant proteins are localized to the nucleus of virus-infected Spodoroptera frugiperda (sf) insect cells and can be recovered as soluble factors. The virus-produced proteins exhibit high-affinity binding to a muscle-specific DNA sequence in the presence of the ubiquitous helix-loop-helix (HLH) protein E12, but only marginal binding in unsupplemented sf nuclear extracts. Both baculovirus-encoded myogenic factors are able to heterooligomerize with E12 in the absence of DNA-binding sites. We conclude from our results that these muscle-specific HLH proteins produced in eucaryotic cells largely depend on dimerization with E12 or similar HLH proteins to recognize the myosin-light-chain-enhancer-MEF-1-binding site. We have no evidence for intracellular protein modifications exerting major effects on the interaction between these factors and DNA.

Original languageEnglish (US)
Pages (from-to)187-193
Number of pages7
JournalEuropean Journal of Biochemistry
Volume198
Issue number1
StatePublished - 1991

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Myosin Light Chains
Baculoviridae
Viruses
Muscle
Proteins
Binding Sites
Transcription Factor 3
Myogenin
Muscles
Dimerization
DNA sequences
DNA
Recombinant Proteins
Insects

ASJC Scopus subject areas

  • Biochemistry

Cite this

Baculovirus-expressed myogenic determination factors require E12 complex formation for binding to the myosin-light-chain enhancer. / Braun, T.; Gearing, K.; Wright, W. E.; Arnold, H. H.

In: European Journal of Biochemistry, Vol. 198, No. 1, 1991, p. 187-193.

Research output: Contribution to journalArticle

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