The Vesicle-inducing Protein 1 from Synechocystis sp. PCC 6803 Organizes into Diverse Higher-Ordered Ring Structures

Publication type:
Journal article
Metadata:
Abstract
<jats:p>The vesicle-inducing protein in plastids 1 (Vipp1) was found to be involved in thylakoid membrane formation in chloroplasts and cyanobacteria. In contrast to chloroplasts, it has been suggested that in cyanobacteria the protein is only tightly associated with the cytoplasmic membrane. In the present study we analyze and describe the subcellular localization and the oligomeric organization of Vipp1 from the cyanobacterium Synechocystis PCC 6803. Vipp1 forms stable dimers and higher-ordered oligomers in the cytoplasm as well as at both the cytoplasmic and thylakoid membrane. Vipp1 oligomers are organized in ring structures with a variable diameter of 25–33 nm and corresponding calculated molecular masses of ∼1.6–2.2 MDa. Six different types of rings were found with an unusual 12–17-fold symmetrical conformation. The simultaneous existence of multiple types of rings is very unusual and suggests a special function of Vipp1. Involvement of diverse ring structures in vesicle formation is suggested.</jats:p>
Autoren
  • Eva Fuhrmann
  • Jelle B Bultema
  • Uwe Kahmann
  • Eva Rupprecht
  • Egbert J Boekema
  • Dirk Schneider
DOI
10.1091/mbc.e09-04-0319
Editoren
  • Reid Gilmore
eISSN
1939-4586
ISSN
1059-1524
Ausgabe der Veröffentlichung
21
Zeitschrift
Molecular Biology of the Cell
Sprache
en
Paginierung
4620 - 4628
Datum der Veröffentlichung
2009
Status
Published
Herausgeber
American Society for Cell Biology (ASCB)
Herausgeber URL
http://dx.doi.org/10.1091/mbc.e09-04-0319
Datum der Datenerfassung
2021
Titel
The Vesicle-inducing Protein 1 from Synechocystis sp. PCC 6803 Organizes into Diverse Higher-Ordered Ring Structures
Ausgabe der Zeitschrift
20

Data source: Crossref

Other metadata sources:
Abstract
The vesicle-inducing protein in plastids 1 (Vipp1) was found to be involved in thylakoid membrane formation in chloroplasts and cyanobacteria. In contrast to chloroplasts, it has been suggested that in cyanobacteria the protein is only tightly associated with the cytoplasmic membrane. In the present study we analyze and describe the subcellular localization and the oligomeric organization of Vipp1 from the cyanobacterium Synechocystis PCC 6803. Vipp1 forms stable dimers and higher-ordered oligomers in the cytoplasm as well as at both the cytoplasmic and thylakoid membrane. Vipp1 oligomers are organized in ring structures with a variable diameter of 25-33 nm and corresponding calculated molecular masses of approximately 1.6-2.2 MDa. Six different types of rings were found with an unusual 12-17-fold symmetrical conformation. The simultaneous existence of multiple types of rings is very unusual and suggests a special function of Vipp1. Involvement of diverse ring structures in vesicle formation is suggested.
Addresses
  • Institut für Biochemie und Molekularbiologie, ZBMZ, Albert-Ludwigs-Universität, 79104 Freiburg, Germany.
Autoren
  • Eva Fuhrmann
  • Jelle B Bultema
  • Uwe Kahmann
  • Eva Rupprecht
  • Egbert J Boekema
  • Dirk Schneider
DOI
10.1091/mbc.e09-04-0319
eISSN
1939-4586
Externe Identifier
  • PubMed Identifier: 19776353
  • PubMed Central ID: PMC2770949
Open access
false
ISSN
1059-1524
Ausgabe der Veröffentlichung
21
Zeitschrift
Molecular biology of the cell
Schlüsselwörter
  • Intracellular Membranes
  • Cytoplasmic Vesicles
  • Thylakoids
  • Synechocystis
  • Bacterial Proteins
  • Membrane Proteins
  • Protein Structure, Quaternary
  • Protein Multimerization
Sprache
eng
Medium
Print-Electronic
Online publication date
2009
Paginierung
4620 - 4628
Datum der Veröffentlichung
2009
Status
Published
Datum der Datenerfassung
2009
Titel
The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structures.
Sub types
  • Research Support, Non-U.S. Gov't
  • research-article
  • Journal Article
Ausgabe der Zeitschrift
20

Files

http://www.molbiolcell.org/cgi/reprint/20/21/4620.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19776353/pdf/?tool=EBI https://europepmc.org/articles/PMC2770949?pdf=render

Data source: Europe PubMed Central

Abstract
The vesicle-inducing protein in plastids 1 (Vipp1) was found to be involved in thylakoid membrane formation in chloroplasts and cyanobacteria. In contrast to chloroplasts, it has been suggested that in cyanobacteria the protein is only tightly associated with the cytoplasmic membrane. In the present study we analyze and describe the subcellular localization and the oligomeric organization of Vipp1 from the cyanobacterium Synechocystis PCC 6803. Vipp1 forms stable dimers and higher-ordered oligomers in the cytoplasm as well as at both the cytoplasmic and thylakoid membrane. Vipp1 oligomers are organized in ring structures with a variable diameter of 25-33 nm and corresponding calculated molecular masses of approximately 1.6-2.2 MDa. Six different types of rings were found with an unusual 12-17-fold symmetrical conformation. The simultaneous existence of multiple types of rings is very unusual and suggests a special function of Vipp1. Involvement of diverse ring structures in vesicle formation is suggested.
Autoren
  • Eva Fuhrmann
  • Jelle B Bultema
  • Uwe Kahmann
  • Eva Rupprecht
  • Egbert J Boekema
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/19776353
DOI
10.1091/mbc.e09-04-0319
eISSN
1939-4586
Externe Identifier
  • PubMed Central ID: PMC2770949
Ausgabe der Veröffentlichung
21
Zeitschrift
Mol Biol Cell
Schlüsselwörter
  • Bacterial Proteins
  • Cytoplasmic Vesicles
  • Intracellular Membranes
  • Membrane Proteins
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Synechocystis
  • Thylakoids
Sprache
eng
Country
United States
Paginierung
4620 - 4628
PII
E09-04-0319
Datum der Veröffentlichung
2009
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2010
Titel
The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structures.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
20

Data source: PubMed

Beziehungen:
Property of

Tools