PMID:9137831

Citation	Fushimi, K, Bai, L, Marumo, F and Sasaki, S (1997) Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia coli. Biochem. Mol. Biol. Int. 41:995-1003
Abstract	Members of the membrane intrinsic protein (MIP) family are expressed in various organisms including plants, insects, and vertebrates. E. coli is known to have a MIP member gene, glycerol facilitator (G1pF). Here we report the isolation of E. coli gene encoding BniP, bacterial nodulin-like intrinsic protein. BniP encodes a 231 amino acid, 24 kDa protein with 42% amino acid identity to Nod26, 38% amino acid identity to AQP1, and 29% amino acid identity to G1pF. Analysis of deduced amino acid sequence predicted a hydrophobic protein with six membrane-spanning domains. Expression of BniP in Xenopus oocytes induced slight increase in osmotic water permeability, but not glycerol or ion permeability. Our results showed that BniP is a new member of the MIP channel-forming proteins of E. coli.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Aquaporins; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Blotting, Southern; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Genes, Bacterial; Genome, Bacterial; Membrane Proteins; Molecular Sequence Data; Polymerase Chain Reaction; Sequence Homology, Amino Acid; Xenopus
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