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Tytuł:
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Coordinate expression of a small polypeptide with the lactose carrier of Escherichia coli.
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Autorzy:
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Lagarias DM
Villarejo M
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Źródło:
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The Journal of biological chemistry [J Biol Chem] 1985 Nov 15; Vol. 260 (26), pp. 14235-41.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
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Język:
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English
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Imprint Name(s):
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Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
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MeSH Terms:
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Escherichia coli Proteins*
Lac Operon*
Monosaccharide Transport Proteins*
Symporters*
Bacterial Proteins/*genetics
Escherichia coli/*genetics
Amino Acid Sequence ; Bacterial Proteins/isolation & purification ; Base Sequence ; DNA, Bacterial ; Immunologic Techniques ; Membrane Proteins/genetics ; Membrane Transport Proteins/genetics ; Molecular Weight ; Nucleic Acid Hybridization ; Plasmids ; RNA, Bacterial/genetics ; RNA, Messenger/genetics ; Transcription, Genetic
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Grant Information:
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GM-23189 United States GM NIGMS NIH HHS
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Substance Nomenclature:
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0 (Bacterial Proteins)
0 (DNA, Bacterial)
0 (Escherichia coli Proteins)
0 (LacY protein, E coli)
0 (Membrane Proteins)
0 (Membrane Transport Proteins)
0 (Monosaccharide Transport Proteins)
0 (RNA, Bacterial)
0 (RNA, Messenger)
0 (Symporters)
9068-45-5 (lactose permease)
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Entry Date(s):
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Date Created: 19851115 Date Completed: 19851213 Latest Revision: 20210210
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Update Code:
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20240104
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PMID:
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2414292
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Induction of the lac operon in wild type Escherichia coli strains results in synthesis of a 16-kDa inner membrane protein in addition to the known products of the lacZ, lacY, and lacA genes. Cells carrying the lacY gene on a multicopy plasmid overproduce this 16-kDa polypeptide as well as the Lac carrier, the membrane protein product of the lacY gene. However, [35S]methionine labeling of minicells carrying the lacY plasmid shows that the 16-kDa protein is not synthesized from the plasmid DNA. We have purified and partially characterized the 16-kDa protein. It is an acidic membrane protein of apparent Mr = 15,800 whose amino-terminal sequence (NH2-Met-Arg-Asn-Phe-Asp-Leu-) does not match any known lac operon DNA sequence. Using antibody prepared to the purified 16-kDa protein, we have quantitatively analyzed conditions under which this protein is made and have shown that the amount of 16-kDa protein which appears in the membrane is proportional to lac operon expression. Hybridization of a synthetic oligodeoxyribonucleotide probe complementary to the 5' end of 16-kDa protein mRNA shows that its synthesis is regulated at the level of transcription.