doi: 10.1073/pnas.81.23.7333.
ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system
- PMID: 6239289
- PMCID: PMC392140
- DOI: 10.1073/pnas.81.23.7333
Item in Clipboard
ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system
Proc Natl Acad Sci U S A.
1984 Dec.
Abstract
Two components of the histidine permease in Salmonella typhimurium, the membrane-bound P and M proteins, react with the photoaffinity labeling reagent 8-azido-ATP in isolated membranes. The extent of labeling is decreased by the addition of ATP and somewhat less by addition of GTP, CTP, UTP, and ADP. Cyclic AMP, NAD, FAD, and S-adenosylmethionine have little effect. We propose that one or both of these proteins have a site capable of binding an adenine nucleotide and that, therefore, they may be involved in the energy-coupling step in active transport.
Similar articles
-
Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport.Proc Natl Acad Sci U S A. 1989 Sep;86(18):6953-7. doi: 10.1073/pnas.86.18.6953. Proc Natl Acad Sci U S A. 1989. PMID: 2674940 Free PMC article.
-
The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):620-4. doi: 10.1073/pnas.90.2.620. Proc Natl Acad Sci U S A. 1993. PMID: 7678461 Free PMC article.
-
The nucleotide-binding site of HisP, a membrane protein of the histidine permease. Identification of amino acid residues photoaffinity labeled by 8-azido-ATP.J Biol Chem. 1990 Nov 15;265(32):19535-42. J Biol Chem. 1990. PMID: 2246240
-
Energy coupling in periplasmic permeases: the histidine permease as a model system.Res Microbiol. 1990 Mar-Apr;141(3):341-8. doi: 10.1016/0923-2508(90)90009-f. Res Microbiol. 1990. PMID: 2177913 Review. No abstract available.
-
Subunit interactions in ABC transporters: towards a functional architecture.FEMS Microbiol Lett. 1999 Oct 15;179(2):187-202. doi: 10.1111/j.1574-6968.1999.tb08727.x. FEMS Microbiol Lett. 1999. PMID: 10518715 Review.
Cited by
-
A new cell division operon in Escherichia coli.Mol Gen Genet. 1986 Oct;205(1):134-45. doi: 10.1007/BF02428043. Mol Gen Genet. 1986. PMID: 3025556
-
Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems.EMBO J. 1985 Apr;4(4):1033-9. doi: 10.1002/j.1460-2075.1985.tb03735.x. EMBO J. 1985. PMID: 3926486 Free PMC article.
-
Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease.J Bioenerg Biomembr. 2001 Apr;33(2):79-92. doi: 10.1023/a:1010797029183. J Bioenerg Biomembr. 2001. PMID: 11456221
-
Cloning and nucleotide sequence of the chlD locus.J Bacteriol. 1987 May;169(5):1911-6. doi: 10.1128/jb.169.5.1911-1916.1987. J Bacteriol. 1987. PMID: 3553151 Free PMC article.
-
Structural model of the nucleotide-binding conserved component of periplasmic permeases.Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):84-8. doi: 10.1073/pnas.88.1.84. Proc Natl Acad Sci U S A. 1991. PMID: 1986384 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
