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 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.
Inoue
H
H
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka, Japan.
Takahashi
S
S
Fukui
K
K
Miyake
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002238:Carbohydrate Epimerases; D002352:Carrier Proteins / Q000235:genetics*; D005786:Gene Expression Regulation; D006801:Humans; D007668:Kidney / Q000737:chemistry; D016350:Leucine Zippers / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D011108:Polymers; D011233:Precipitin Tests; D051381:Rats; D012083:Renin / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014982:Xenopus laevis / Q000235:genetics
D002352:Carrier Proteins; D011108:Polymers; D012083:Renin; D002238:Carbohydrate Epimerases; C024519:N-acyl-D-glucosamine 2-epimerase; C498259:RENBP protein, human; C498234:Renbp protein, mouse; C498258:Renbp protein, rat