MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer

Lassar, Andrew B.; Buskin, Jean N.; Lockshon, Daniel; Davis, Robert L.; Apone, Stephen; Hauschka, Stephen D.; Weintraub, Harold

doi:10.1016/0092-8674(89)90935-5

Cited by 820 publications

(553 citation statements)

References 25 publications

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“…Nevertheless, the enhancer and p53 elements combined induced the transcription of MCK in a cooperative manner (Figure 5a). At least two elements of de®ned transcription factors are found in the enhancer, MEF2 and MyoD (Lassar et al, 1989;Gossett et al, 1989). Each element was separately placed with the distal p53 element to control a minimal MCK reporter gene (Figure 5b).…”

Section: Discussionmentioning

confidence: 99%

“…MCK gene exhibits the same pattern of expression as that of MLC2 (data not shown; see Figure 1). One transcription factor that participates in MCK transcription is MyoD whose activity is induced at early stages of di erentiation (Lassar et al, 1989). To study the potential role of p53 in the activation of MCK, a DNA fragment of 59 base pairs, containing the distal p53 element of MCK (Zambetti et al, 1992), was used as a probe for DNA binding of p53 from protein extracts derived from C2 cells at di erent stages of di erentiation.…”

Section: Wild Type P53 Protein Is Expressed and Stabilized In DI Erenmentioning

confidence: 99%

“…At least two elements of de®ned transcription factors constitute the MCK enhancer; MEF2 and MyoD (Gossett et al, 1989;Lassar et al, 1989). Reporter genes that contained each of these sites in conjunction with the p53 distal element were constructed and used in transfection studies of 10T1/2 cells.…”

Section: Dominant Negative P53 Inhibits the Expression Of Mckmentioning

confidence: 99%

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p53 protein is activated during muscle differentiation and participates with MyoD in the transcription of muscle creatine kinase gene

Tamir

Bengal

1998

Oncogene

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The p53 protein is a transcription factor involved in processes of cell growth and di erentiation. The muscle creatine kinase (MCK) gene whose transcription is induced during muscle di erentiation contains p53-binding sites. In this study we tested the involvement of p53 in the activation of MCK transcription during muscle di erentiation of C2 cells. We have shown that the p53 protein is stabilized and its DNA binding and transcriptional activities are induced during muscle di erentiation. At the stage of muscle-di erentiation, p53 protein can induce the accurate transcription of a minimal p53-dependent MCK reporter gene. Moreover, p53 cooperates with MyoD in the induction of MCK transcription. The expression of a dominant negative p53 protein in muscle cells reduced the expression of endogenous MCK gene. The dominant negative p53 protein abolished the cooperativity of wild type p53 with MyoD. Amino and carboxy terminal residues of MyoD required for the cooperation with p53 in transcription were identi®ed. The cooperativity between the two proteins occurs also at the stage of DNA binding. We suggest that p53 protein is activated during myoblast di erentiation and participates with MyoD in the induction of MCK transcription.

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Section: Discussionmentioning

confidence: 99%

Section: Wild Type P53 Protein Is Expressed and Stabilized In DI Erenmentioning

confidence: 99%

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p53 protein is activated during muscle differentiation and participates with MyoD in the transcription of muscle creatine kinase gene

Tamir

Bengal

1998

Oncogene

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“…In addition, we have also anaiyzcd mRN.4 levels for three muscle-specific genes, MCK, a-actin and muscle dystrophin, all of which are developmentally regulated. Of these three proteins, MCK was shown to be trans-activated by MyoDl and myogenin [19,20]. Muscle dystrophin is one of the dystrophin isoforms which is distributed along muscle fibers and shows a high concentration in the junctional folds [27,28].…”

Section: Introductionmentioning

confidence: 99%

Changes in the expression of mRNAs for myogenic factors and other muscle‐specific proteins in experimental autoimmune myasthenia gravis

et al. 1992

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The regulation of genes for acetylcholine receptor (AChR), myogenic factors and other muscle‐specific proteins has been analyzed in experimental autoimmune myasthenia gravis (EAMG) and following denervation. The levels of the transcripts for the myogenic factors, MyoDl, myogenin and MRF4, were measured using Northern blot analysis. Myogenin and MRF4 transcript levels were observed to be 3.1 ‐ and 2.6‐fold higher in muscle of rats with EAMG than in controls, respectively. MyoDl levels, however, remained unchanged. The increases in AChR, myogenin and MRF4 mRNAs were one order of magnitude higher in 2‐week denervated muscle than in the myasthenic muscle. The levels of muscle creatine kinase (MCK), α‐actin and muscle dystrophin transcripts were also analyzed. Dystrophin levels were found to be 1.7‐ and 4.7‐fold higher in EAMG and denervated muscle, respectively, than in controls; in contrast, MCK and α‐actin levels remained unchanged.

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“…This putative upstream regulatory element functioned independently of orientation and distance from the promoter, and therefore exhibited the properties of an enhancer. In this region no Myo DI binding sequence [14] or CArG box [15] was found. Instead an AT-rich sequence, so-called MEF-2 binding sequence [16,17], was observed (Fig.…”

Section: A Muscle-specific Enhancer In the M Pronlotermentioning

confidence: 94%

Analysis of upstream regulatory regions required for the activities of two promoters of the rat aldolase A gene

et al. 1991

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Rat aldolase A gene has 2 promoters with different tissue specificities (M-and AH promoters). The M promoter is active only in adult skeletal muscle and induced during myogenesis, whereas the AH promoter is active ubiquitously in many tissues, including various cancer cells. Regulatory sequences for these promoters were investigated through assays for transient expression after introduction into myogenic and nonmyogenic cells. When M promoter-CAT fusion genes were transfected into primary cultures of chicken myoblasts, expression of CAT activity was drastically induce d during myotube formation. The region comprising 202 to 85 base pairs (bp) upstream from the transcription initiation site was found to be necessary for the induction and an enhancer activity whose region includes the AT-rich recognition sequence (MEF-2 binding site). On the other hand. 2 upstream regions were found to be responsible for AH promoter activity expressed in HepG2 cells. The distal region (-280 to -260) of the promoter includes the API binding sequence, whereas the proximal region (-207 to -180) contains a novel inverted repeat consisting of 22 bp but does not contain known promoter and enhancer sequences.

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MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer

Cited by 820 publications

References 25 publications

p53 protein is activated during muscle differentiation and participates with MyoD in the transcription of muscle creatine kinase gene

p53 protein is activated during muscle differentiation and participates with MyoD in the transcription of muscle creatine kinase gene

Changes in the expression of mRNAs for myogenic factors and other muscle‐specific proteins in experimental autoimmune myasthenia gravis

Analysis of upstream regulatory regions required for the activities of two promoters of the rat aldolase A gene

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