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TRIADs: A new class of proteins with a novel cysteine-rich signature

Published online by Cambridge University Press:  01 July 1999

BERT A. VAN DER REIJDEN ,
CLAUDIA A.J. ERPELINCK-VERSCHUEREN ,
BOB LÖWENBERG  and
JOOP H. JANSEN
BERT A. VAN DER REIJDEN
Affiliation:
Institute of Hematology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
CLAUDIA A.J. ERPELINCK-VERSCHUEREN
Affiliation:
Institute of Hematology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
BOB LÖWENBERG
Affiliation:
Institute of Hematology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
JOOP H. JANSEN
Affiliation:
Institute of Hematology, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
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Abstract

Triad1 was recently identified as a nuclear RING finger protein, which is up-regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine-rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C-x(4)-C-x(14–30)-C-x(1–4)-C-x(4)-C-x(2)-C-x(4)-H-x(4)-C defines this structure as the fourth family member of the zinc-binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.

Keywords

LAP/PHD domainLIM domainprotein–DNA interactionprotein–protein interactionRING finger
Type
ACCELERATED COMMUNICATION
Information
Protein Science , Volume 8 , Issue 7 , July 1999 , pp. 1557 - 1561
Copyright
© 1999 The Protein Society

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