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The yeast DNA repair proteins RAD1 and RAD7 share similar putative functional domains
Author(s) -
Schneider Rainer,
Schweiger Manfred
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80588-t
Subject(s) - biology , tandem repeat , dna , yeast , leucine rich repeat , dna repair , angiogenin , genetics , computational biology , biochemistry , microbiology and biotechnology , receptor , gene , genome , angiogenesis
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].