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cDNA-derived amino acid sequence of the NADH-binding 51-kDa subunit of the bovine respiratory NADH dehydrogenase reveals striking similarities to a bacterial NAD(+)-reducing hydrogenase

Patel, Salil D. and Aebersold, Ruedi and Attardi, Giuseppe (1991) cDNA-derived amino acid sequence of the NADH-binding 51-kDa subunit of the bovine respiratory NADH dehydrogenase reveals striking similarities to a bacterial NAD(+)-reducing hydrogenase. Proceedings of the National Academy of Sciences of the United States of America, 88 (10). pp. 4225-4229. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:PATpnas91

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Abstract

A lambda-gt10 bovine brain and a lambda-gt11 bovine heart cDNA library were screened with oligonucleotide probes corresponding to partial protein sequences directly determined from the isolated 51-kDa subunit of the bovine respiratory-chain NADH dehydrogenase. Clones were isolated that encode a protein of 464 amino acids containing all the 11 partial tryptic peptide sequences determined from the 51-kDa subunit. The size and amino acid composition of this protein agree with those determined for the purified 51-kDa subunit. Furthermore, this protein contains a putative NADH-binding domain, a possible FMN-binding site, and a putative binding site for an iron-sulfur cluster. The above evidence indicates that the cloned protein is the 51-kDa subunit or its precursor. A search for sequence similarity with proteins in the Protein Identification Resource data base has revealed that the 51-kDa subunit has 32% amino acid sequence identity with a major portion of the alpha-subunit of the soluble NAD+-reducing hydrogenase from Alcaligenes eutrophus. In particular, there are three segments of high sequence similarity (70-88%) between the two proteins which correspond to the three ligand-binding sites.


Item Type:Article
Additional Information:Copyright © 1991 by the National Academy of Sciences. Contributed by Giuseppe Attardi, January 22, 1991. We are greatly indebted to C. I. Ragan for providing us with a preparation of complex I, to R. Miake-Lye and M. Simon for the λgt10 bovine brain library, to Anne Chomyn for gifts of RNA, and to L. Simpson (University of California, Los Angeles) for the hydropathy plot. We also want to express our appreciation to Anne Chomyn for her help in the early phase of the work and useful discussions and to Russell Doolittle (University of California, San Diego) for valuable comments on the manuscript. The technical assistance of Ms. S. L. Lai, Ms. A. Drew, Ms. L. Tefo, and T. Bures is gratefully acknowledged. These investigations were supported by National Institutes of Health Grant GM11726 to G.A., Medical Research Council of Canada Grant MT-10868 and scholarship to R.A., and a Procter & Gamble fellowship to S.P. The sequence reported in this paper has been deposited in the GenBank data base (accession no. M63009). The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Subject Keywords:Akaligenes eutrophus, mRNA levels in tissues, human genonic sequences
Record Number:CaltechAUTHORS:PATpnas91
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:PATpnas91
Alternative URL:http://www.pnas.org/cgi/content/abstract/88/10/4225
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1246
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:06 Jan 2006
Last Modified:26 Dec 2012 08:43

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