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Nucleic Acids Research, 1994, Vol. 22, No. 6 946-952
© 1994

COMPUTATIONAL BIOLOGY

Evidence for a protein domain superfamily shared by the cyclins, TFIIB and RB/p107

Toby J. Gibson*, Julie D. Thompson, Ariel Blocker and Tony Kouzarides1

European Molecular Biology Laboratory Postfach 102209, Meyerhofstrasse 1, D-69012 Heidelberg, Germany 1Wellcome/CRC Institute, University of Cambridge Tennis Court Road, Cambridge CB2 1QR, UK

*To whom correspondence should be addressed

Received January 6, 1994. Revised February 11, 1994. Accepted February 11, 1994.

Cyclins, TFIIB and RB play major roles in cell cycle and/or gene regulation. Earlier work has suggested common ancestry for the TFIIB repeats and RB pocket B which share 20% sequence Identity. We now report that database searches with profiles based on a multiple alignment of cyclin core regions (the ‘cyclin box’) detect the TFIIB repeats with equivalent scores to divergent cyclins. Several features of the sequences support the notion of common ancestry: e.g. cyclins A/B, C and D share {sum}20 – 30% identity but each have {sum}15 – 20% identity with vertebrate TFIIB, showing that conserved cyclin features underlie the match. These results suggest the presence of a domain superfamily, which we term the TR domain, in nuclear regulatory proteins belonging to the TFIIB, cyclin and RB families, that has been duplicated many times during eukaryotlc evolution. The TR domain appears to function in protein - protein interactions.


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