The yeast DNA repair proteins RAD1 and RAD7 share similar putative functional domains

FEBS Letters

Schweiger, Manfred¹  Schneider, Rainer¹ 

[1] Institut für Biochemie, Universität Innsbruck, Peter Mayr Str. 1a, A-6020 Innsbruck, Austria

关键词: DNA repair;    RAD1;    RAD7;    Leucine-rich motif;    Protein-protein interaction;    Superfamily;   

DOI  :  10.1016/0014-5793(91)80588-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sequence information on eukaryotic DNA repair proteins provided so far only few clues concerning possible functional domains. Since the DNA repair process involves a strict sequential complex formation of several proteins [(1988) FASEB J. 2, 2696–2701], we searched for special protein-protein interacting domains, which consist of tandemly repeated leucine rich motifs (LRM). Search algorithms, capable of detecting even largely divergent repeats by assessing their significance due to the tandem repetitivity, revealed that the yeast DNA repair proteins RAD1 and RAD7 contain 9 and 12 tandem LRM repeats, respectively. These results represent the first clues concerning specific domains in these proteins and assign them to the LRM superfamily, which includes such members as yeast adenylate cyclase, cell surface protein receptors and ribonuclease/angiogenin inhibitor, all exerting their function by specific protein-protein interactions involving LRM domains [(1988) EMBO J. 7, 4151–4156; (1990) Proc. Natl. Acad. Sci. USA 87, 8711–8715; (1989) Science 245, 494–499; (1990) Mol. Cell. Biol. 10, 6436–6444; (1989) Proc. Natl. Acad. Sci. USA 86, 6773–6777].

【 授权许可】

Unknown