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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.


European Journal of Biochemistry 198 (1991), No.1, pp.187-193
ISSN: 0014-2956
Journal Article
Fraunhofer ITA ( ITEM) ()
baculoviridae; gene expression; genetic; genetic transcription; muscle; muscle protein; myosin; regulation

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 interac tion between these factors and DNA.