Structural properties of the proton translocating complex of the clathrin-coated vesicle.

D. K. Stone, S. Z. Sun, X. S. Xie

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The clathrin-coated vesicle proton pump is a representative member of the new class of endomembrane proton ATPases that share an inhibitor profile which distinguishes them from classic F1F0 and E1E2-type proton pumps. The coated vesicle proton pump is a large (530 kDa) heteroligomer composed of eight polypeptides with molecular masses of 116, 70, 58, 40, 38, 34, 33 and 17 kDa. The 200-fold purified enzyme catalyses ATP-generated proton pumping when reconstituted in liposomes composed of pure lipids. Subunit function has been determined by partial reaction analysis of subunit and subcomplex activities. The isolated 17 kDa subunit, when co-reconstituted with bacteriorhodopsin, forms a dicyclohexylcarbodiimide-inhibitable proton channel. Selective removal of the 116 kDa subunit transforms the proton ATPase from a Mg2+-activatable to a Ca2+-activatable ATPase. Subsequent dissociation and reconstitution of subunits reveals that the 70, 58, 40 and 33 kDa components are required, in composite, to form a functional ATP-hydrolytic core, and that no single subunit or subcomplex deficient in these subunits can catalyse ATP hydrolysis.

Original languageEnglish (US)
Pages (from-to)238-251
Number of pages14
JournalCiba Foundation symposium
Volume139
StatePublished - 1988

Fingerprint

Clathrin-Coated Vesicles
Proton Pumps
Protons
Adenosine Triphosphate
Coated Vesicles
Dicyclohexylcarbodiimide
Bacteriorhodopsins
Ca(2+) Mg(2+)-ATPase
Calcium-Transporting ATPases
Liposomes
Adenosine Triphosphatases
Hydrolysis
Lipids
Peptides
Enzymes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Structural properties of the proton translocating complex of the clathrin-coated vesicle. / Stone, D. K.; Sun, S. Z.; Xie, X. S.

In: Ciba Foundation symposium, Vol. 139, 1988, p. 238-251.

Research output: Contribution to journalArticle

@article{9c1b060cd3f54993aa4cb0dd6b04724c,
title = "Structural properties of the proton translocating complex of the clathrin-coated vesicle.",
abstract = "The clathrin-coated vesicle proton pump is a representative member of the new class of endomembrane proton ATPases that share an inhibitor profile which distinguishes them from classic F1F0 and E1E2-type proton pumps. The coated vesicle proton pump is a large (530 kDa) heteroligomer composed of eight polypeptides with molecular masses of 116, 70, 58, 40, 38, 34, 33 and 17 kDa. The 200-fold purified enzyme catalyses ATP-generated proton pumping when reconstituted in liposomes composed of pure lipids. Subunit function has been determined by partial reaction analysis of subunit and subcomplex activities. The isolated 17 kDa subunit, when co-reconstituted with bacteriorhodopsin, forms a dicyclohexylcarbodiimide-inhibitable proton channel. Selective removal of the 116 kDa subunit transforms the proton ATPase from a Mg2+-activatable to a Ca2+-activatable ATPase. Subsequent dissociation and reconstitution of subunits reveals that the 70, 58, 40 and 33 kDa components are required, in composite, to form a functional ATP-hydrolytic core, and that no single subunit or subcomplex deficient in these subunits can catalyse ATP hydrolysis.",
author = "Stone, {D. K.} and Sun, {S. Z.} and Xie, {X. S.}",
year = "1988",
language = "English (US)",
volume = "139",
pages = "238--251",
journal = "CIBA Foundation Symposia",
issn = "0300-5208",
publisher = "Wiley Subscription Services",

}

TY - JOUR

T1 - Structural properties of the proton translocating complex of the clathrin-coated vesicle.

AU - Stone, D. K.

AU - Sun, S. Z.

AU - Xie, X. S.

PY - 1988

Y1 - 1988

N2 - The clathrin-coated vesicle proton pump is a representative member of the new class of endomembrane proton ATPases that share an inhibitor profile which distinguishes them from classic F1F0 and E1E2-type proton pumps. The coated vesicle proton pump is a large (530 kDa) heteroligomer composed of eight polypeptides with molecular masses of 116, 70, 58, 40, 38, 34, 33 and 17 kDa. The 200-fold purified enzyme catalyses ATP-generated proton pumping when reconstituted in liposomes composed of pure lipids. Subunit function has been determined by partial reaction analysis of subunit and subcomplex activities. The isolated 17 kDa subunit, when co-reconstituted with bacteriorhodopsin, forms a dicyclohexylcarbodiimide-inhibitable proton channel. Selective removal of the 116 kDa subunit transforms the proton ATPase from a Mg2+-activatable to a Ca2+-activatable ATPase. Subsequent dissociation and reconstitution of subunits reveals that the 70, 58, 40 and 33 kDa components are required, in composite, to form a functional ATP-hydrolytic core, and that no single subunit or subcomplex deficient in these subunits can catalyse ATP hydrolysis.

AB - The clathrin-coated vesicle proton pump is a representative member of the new class of endomembrane proton ATPases that share an inhibitor profile which distinguishes them from classic F1F0 and E1E2-type proton pumps. The coated vesicle proton pump is a large (530 kDa) heteroligomer composed of eight polypeptides with molecular masses of 116, 70, 58, 40, 38, 34, 33 and 17 kDa. The 200-fold purified enzyme catalyses ATP-generated proton pumping when reconstituted in liposomes composed of pure lipids. Subunit function has been determined by partial reaction analysis of subunit and subcomplex activities. The isolated 17 kDa subunit, when co-reconstituted with bacteriorhodopsin, forms a dicyclohexylcarbodiimide-inhibitable proton channel. Selective removal of the 116 kDa subunit transforms the proton ATPase from a Mg2+-activatable to a Ca2+-activatable ATPase. Subsequent dissociation and reconstitution of subunits reveals that the 70, 58, 40 and 33 kDa components are required, in composite, to form a functional ATP-hydrolytic core, and that no single subunit or subcomplex deficient in these subunits can catalyse ATP hydrolysis.

UR - http://www.scopus.com/inward/record.url?scp=0024248205&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024248205&partnerID=8YFLogxK

M3 - Article

C2 - 2462480

AN - SCOPUS:0024248205

VL - 139

SP - 238

EP - 251

JO - CIBA Foundation Symposia

JF - CIBA Foundation Symposia

SN - 0300-5208

ER -