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Protein Science, Vol 7, Issue 5 1250-1254, Copyright © 1998 by Cold Spring Harbor Laboratory Press
FOR THE RECORD |
L. ARAVIND and C. P. PONTING
Department of Biology-BSBW, Texas A&M University, College Station, Texas 77843 Current address: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bldg. 38A, Bethesda, Maryland 20894.
Single copies of an {alpha}-helical-rich motif are demonstrated to be present within subunits of the large multiprotein 26S proteasome and eukaryotic initiation factor-3 (eIF3) complexes, and within proteins involved in transcriptional regulation. In addition, p40 and p47 subunits of eIF3 are shown to be homologues of the proteasome subunit Mov34, and transcriptional regulators JAB1/pad1. Finally, the proteasome subunit S5a and the p44 subunit of the basal transcription factor IIH (TFIIH) are identified as homologues. The presence of homologous, and sometimes identical, proteins in contrasting functional contexts suggests that the large multisubunit complexes of the 26S proteasome, eIF3 and TFIIH perform overlapping cellular roles.
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