Leucine zipper motif in porcine renin-binding protein (RnBP) and its relationship to the formation of an RnBP-renin heterodimer and an RnBP homodimer
An apparent leucine zipper motif was recognized in the predicted amino acid sequence of porcine kidney renin-binding protein (RnBP) by analysis of the nucleotide sequence of a cDNA encoding the protein (Inoue, H., Fukui, K., Takahashi, S., and Miyake, Y. (1990) J. Biol. Chem. 265, 6556-6561). To eva...
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Published in | The Journal of biological chemistry Vol. 266; no. 18; pp. 11896 - 11900 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
25.06.1991
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Subjects | |
Online Access | Get full text |
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Summary: | An apparent leucine zipper motif was recognized in the predicted amino acid sequence of porcine kidney renin-binding protein
(RnBP) by analysis of the nucleotide sequence of a cDNA encoding the protein (Inoue, H., Fukui, K., Takahashi, S., and Miyake,
Y. (1990) J. Biol. Chem. 265, 6556-6561). To evaluate the role of this motif in the formation of an RnBP-renin heterodimer
and an RnBP homodimer, a porcine mutant cDNA involving Leu185---Asp and Leu192---Asp substitutions was constructed and expressed
in vitro and in Xenopus oocytes. The mutant protein neither binds to renin nor forms the homodimer. The results strongly suggest
that the leucine zipper motif in the RnBP molecule mediates the formation of both the RnBP-renin heterodimer and the RnBP
homodimer observed previously. The existence of the motif should facilitate elucidation of the role of RnBP in renin metabolism. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/s0021-9258(18)99042-3 |