The ATP synthase of Escherichia coli: structure and function of F-0 subunits

Autor(en): Deckers-Hebestreit, G 
Greie, JC
Stalz, WD
Altendorf, K 
Stichwörter: ALPHA-SUBUNIT; B-SUBUNIT; Biochemistry & Molecular Biology; Biophysics; BOVINE HEART-MITOCHONDRIA; CARBOXYL-TERMINAL REGION; circular dichroism; CROSS-LINKING; DELTA-SUBUNIT; Escherichia coli; F-0 complex; F0F1-ATPase; F1F0-ATP SYNTHASE; H+-ATPASE; H+/ATP COUPLING RATIO; monoclonal antibody; POLAR LOOP REGION; topology
Erscheinungsdatum: 2000
Herausgeber: ELSEVIER SCIENCE BV
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volumen: 1458
Ausgabe: 2-3
Startseite: 364
Seitenende: 373
Zusammenfassung: 
In this review we discuss recent work from our laboratory concerning the structure and/or function of the F-0 subunits of the proton-translocating ATP synthase of Escherichia coli. For the topology of subunit tr a brief discussion gives (i) a detailed picture of the C-terminal two-thirds of the protein with four transmembrane helices and the C terminus exposed to the cytoplasm and (ii) an evaluation of the controversial results obtained for the localization of the N-terminal region of subunit a including its consequences on the number of transmembrane helices. The structure of membrane-bound subunit b has been determined by circular dichroism spectroscopy to be at least 75% alpha-helical, For this purpose a method was developed, which allows the determination of the structure composition of membrane proteins in protroliposomes. Subunit b, was purified to homogeneity by preparative SDS gel electrophoresis, precipitated with acetone, and redissolved in cholate-containing buffer, thereby retaining its native conformation as shown by functional coreconstitution with an ne subcomplex. Monoclonal antibodies, which have their epitopes located within the hydrophilic loop region of subunit c, and the F-1 part are bound simultaneously to the F-0 complex without an effect on the function of F-0, indicating that not all c subunits are involved in F-1 interaction. Consequences on the coupling mechanism between ATP synthesis/hydrolysis and proton translocation are discussed. (C) 2000 Elsevier Science B.V. All rights reserved.
ISSN: 00052728
DOI: 10.1016/S0005-2728(00)00087-6

Show full item record

Page view(s)

3
Last Week
0
Last month
0
checked on Mar 1, 2024

Google ScholarTM

Check

Altmetric