Defining the Structural Basis for Assembly of a Transmembrane Cytochrome

Publication type:
Journal article
Metadata:
Autoren
  • Alexander Prodöhl
  • Thomas Volkmer
  • Carmen Finger
  • Dirk Schneider
DOI
10.1016/j.jmb.2005.05.016
ISSN
0022-2836
Ausgabe der Veröffentlichung
4
Zeitschrift
Journal of Molecular Biology
Sprache
en
Paginierung
744 - 756
Datum der Veröffentlichung
2005
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.jmb.2005.05.016
Datum der Datenerfassung
2019
Titel
Defining the Structural Basis for Assembly of a Transmembrane Cytochrome
Ausgabe der Zeitschrift
350

Data source: Crossref

Other metadata sources:
Abstract
To define the structural basis for cofactor binding to membrane proteins, we introduce a manageable model system, which allows us, for the first time, to study the influence of individual transmembrane helices and of single amino acid residues on the assembly of a transmembrane cytochrome. In vivo as well as in vitro analyses indicate central roles of single amino acid residues for either interaction of the transmembrane helices or for binding of the cofactor. The results clearly show that interaction of the PsbF transmembrane helix is independent from binding of the heme cofactor. On the other hand, binding of the cofactor highly depends on helix-helix interactions. By site-directed mutagenesis critical amino acid residues were identified, which are involved in the assembly of a functional transmembrane cytochrome. Especially, a highly conserved glycine residue is critical for interaction of the transmembrane helices and assembly of the cytochrome. Based on the two-stage-model of alpha-helical membrane protein folding, the presented results clearly indicate a third stage of membrane protein folding, in which a cofactor binds to a pre-assembled transmembrane protein.
Addresses
  • Institut für Biochemie und Molekularbiologie, Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.
Autoren
  • Alexander Prodöhl
  • Thomas Volkmer
  • Carmen Finger
  • Dirk Schneider
DOI
10.1016/j.jmb.2005.05.016
eISSN
1089-8638
Externe Identifier
  • PubMed Identifier: 15950240
Open access
false
ISSN
0022-2836
Ausgabe der Veröffentlichung
4
Zeitschrift
Journal of molecular biology
Schlüsselwörter
  • Synechocystis
  • Heme
  • Cytochromes
  • Cytochrome b Group
  • Amino Acids
  • Bacterial Proteins
  • Amino Acid Sequence
  • Protein Binding
  • Dimerization
  • Molecular Sequence Data
Sprache
eng
Medium
Print
Paginierung
744 - 756
Datum der Veröffentlichung
2005
Status
Published
Datum der Datenerfassung
2005
Titel
Defining the structural basis for assembly of a transmembrane cytochrome.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
Ausgabe der Zeitschrift
350

Data source: Europe PubMed Central

Abstract
To define the structural basis for cofactor binding to membrane proteins, we introduce a manageable model system, which allows us, for the first time, to study the influence of individual transmembrane helices and of single amino acid residues on the assembly of a transmembrane cytochrome. In vivo as well as in vitro analyses indicate central roles of single amino acid residues for either interaction of the transmembrane helices or for binding of the cofactor. The results clearly show that interaction of the PsbF transmembrane helix is independent from binding of the heme cofactor. On the other hand, binding of the cofactor highly depends on helix-helix interactions. By site-directed mutagenesis critical amino acid residues were identified, which are involved in the assembly of a functional transmembrane cytochrome. Especially, a highly conserved glycine residue is critical for interaction of the transmembrane helices and assembly of the cytochrome. Based on the two-stage-model of alpha-helical membrane protein folding, the presented results clearly indicate a third stage of membrane protein folding, in which a cofactor binds to a pre-assembled transmembrane protein.
Date of acceptance
2005
Autoren
  • Alexander Prodöhl
  • Thomas Volkmer
  • Carmen Finger
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/15950240
DOI
10.1016/j.jmb.2005.05.016
ISSN
0022-2836
Ausgabe der Veröffentlichung
4
Zeitschrift
J Mol Biol
Schlüsselwörter
  • Amino Acid Sequence
  • Amino Acids
  • Bacterial Proteins
  • Cytochrome b Group
  • Cytochromes
  • Dimerization
  • Heme
  • Molecular Sequence Data
  • Protein Binding
  • Synechocystis
Sprache
eng
Country
Netherlands
Paginierung
744 - 756
PII
S0022-2836(05)00547-4
Datum der Veröffentlichung
2005
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2005
Titel
Defining the structural basis for assembly of a transmembrane cytochrome.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
350

Data source: PubMed

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