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Titolo:
The yeast mitochondrial citrate transport protein - Probing the secondary structure of transmembrane domain IV and identification of residues that likely comprise a portion of the citrate translocation pathway
Autore:
Kaplan, RS; Mayor, JA; Brauer, D; Kotaria, R; Walters, DE; Dean, AM;
Indirizzi:
Finch Univ Hlth Sci Chicago Med Sch, Dept Biochem & Mol Biol, N Chicago, IL 60064 USA Finch Univ Hlth Sci Chicago Med Sch N Chicago IL USA 60064 , IL 60064 USA BPTI Gortner Labs 240, St Paul, MN 55108 USA BPTI Gortner Labs 240 St Paul MN USA 55108 abs 240, St Paul, MN 55108 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 16, volume: 275, anno: 2000,
pagine: 12009 - 12016
SICI:
0021-9258(20000421)275:16<12009:TYMCTP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MITOCHONDRIA; MEMBRANE-SPANNING SEGMENT; CHANNEL-LINING RESIDUES; DOPAMINE D2 RECEPTOR; BINDING-SITE CREVICE; FATTY-ACID SYNTHESIS; TRICARBOXYLATE CARRIER; CONDUCTANCE REGULATOR; PURIFICATION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Kaplan, RS Finch Univ Hlth Sci Chicago Med Sch, Dept Biochem & Mol Biol, 3333 Green Bay Rd, N Chicago, IL 60064 USA Finch Univ Hlth Sci Chicago Med Sch 3333 Green Bay Rd N Chicago IL USA 60064
Citazione:
R.S. Kaplan et al., "The yeast mitochondrial citrate transport protein - Probing the secondary structure of transmembrane domain IV and identification of residues that likely comprise a portion of the citrate translocation pathway", J BIOL CHEM, 275(16), 2000, pp. 12009-12016

Abstract

The mitochondrial citrate transport protein (CTP) has been investigated byreplacing 22 consecutive residues within transmembrane domain IV, one at atime, with cysteine. A cysteine-less CTP retaining wild-type functional properties served as the starting template. The single Cys CTP variants were overexpressed in Escherichia coli, isolated, and functionally reconstitutedin a liposomal system. The accessibility of each single Cys mutant to three methanethiosulfonate reagents was evaluated by determining the pseudo first order rate constants for inhibition of CTP function, These rate constants varied by seven orders of magnitude. With three independent data sets we observed peaks and troughs in the rate constant data at identical amino acid positions and a periodicity of four was observed from residues 177-193, Based on the pattern of accessibility we conclude that residues 177-193 exist as an alpha-helix. Furthermore, a water-accessible face of the helix has been defined consisting of Pro-177, Val-178, Arg-181, Gln-182, Asn-185, Gln-186, Arg-189, Leu-190, and Tyr-193, and a water-inaccessible face has beendelineated consisting of Ser-179, Met-180, Ala-183, Ala-184, Ala-187, Val-188, Gly-191, and Ser-192. We infer that the water-accessible face comprises a portion of the substrate translocation pathway through the CTP, whereasthe water-inaccessible surface faces the lipid bilayer.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 15:03:44