Organization of the chick CDC37 gene
CDC37 and the chaperone protein, Hsp90, form a complex that binds to several kinases, resulting in stabilization and promotion of their activity. CDC37 also binds DNA and glycosaminoglycans in a sequence-specific manner. In this study, we further characterize chick CDC37 and examine the organization...
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Veröffentlicht in: | The Journal of biological chemistry 1998-02, Vol.273 (6), p.3598-3603 |
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Sprache: | eng |
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Zusammenfassung: | CDC37 and the chaperone protein, Hsp90, form a complex that binds to several kinases, resulting in stabilization and promotion
of their activity. CDC37 also binds DNA and glycosaminoglycans in a sequence-specific manner. In this study, we further characterize
chick CDC37 and examine the organization of the CDC37 gene. Chick CDC37 is a â¼50-kDa protein encoded by an mRNA of â¼1.7 kilobases.
The CDC37 gene is â¼8.5 kilobases and contains 8 exons and 7 introns of various sizes. The presumptive promoter and 5â²-flanking
regions contain an E2 box and consensus binding sites for SP1, for the S8 homeodomain protein, and for two zinc finger clusters
within the myeloid progenitor transcription factor, MZF1. Particularly striking is a â¼470-base pair region composed of a highly
repetitive 10â11-base pair sequence, (T/C)gCTAT(A/G)GGG(A/T) (where g represents the additional G present in the 11-base pair
sequence). This region includes 15 copies of the sequence, TATGGGGA, which conforms to the DNA consensus sequence recognized
by one of the zinc finger clusters in MZF1. These findings emphasize the potential importance of CDC37 in regulation of cellular
behavior during tissue development and reorganization. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.273.6.3598 |