Nucleic Acids Research, Vol 24, Issue 16 3121-3128, Copyright © 1996 by Oxford University Press
R Goldman-Levi, C Miller, J Bogoch and NB Zak
Many proteins of the SNF2 family, which share a similar DNA-dependent
ATPase/putative helicase domain, are involved in global transcriptional
control and processing of DNA damage. We report here the partial cloning
and characterization of 89B helicase, a gene encoding a new Drosophila
melanogaster member of the SNF2 family. 89B Helicase protein shows a high
degree of homology in its ATPase/helicase domain to the global
transcriptional activators SNF2 and Brahma and to the DNA repair proteins
ERCC6 and RAD54. It is, however, most strikingly similar to the
Saccharomyces cerevisiae protein Mot1, a transcriptional repressor with
many target genes for which no homologue has yet been described. 89B
helicase is expressed throughout fly development and its large transcript
encodes a >200 kDa protein. Staining with anti-89B Helicase antibodies
reveals that the protein is present uniformly in early embryos and then
becomes localized to the ventral nerve cord and brain. On the polytene
chromosomes, 89B Helicase is bound to several hundred specific sites that
are randomly distributed. The homology of 89B Helicase to Mot1, its
widespread developmental expression and its large number of targets on the
polytene chromosomes of larval salivary gland cells suggest that 89B
Helicase may play a role in chromosomal metabolism, particularly global
transcriptional regulation.
ARTICLES
Expanding the Mot1 subfamily: 89B helicase encodes a new Drosophila melanogaster SNF2-related protein which binds to multiple sites on polytene chromosomes
Hubert H. Humphrey Center for Experimental Medicine and Cancer Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
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