Please use this identifier to cite or link to this item:
Authors: Siebenaller, Carmen
Schlösser, Lukas
Junglas, Benedikt
Schmidt-Dengler, Martina
Jacob, Dominik
Hellmann, Nadja
Sachse, Carsten
Helm, Mark
Schneider, Dirk
Title: Binding and/or hydrolysis of purine-based nucleotides is not required for IM30 ring formation
Online publication date: 11-Nov-2022
Year of first publication: 2021
Language: english
Abstract: IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms large oligomeric ring complexes, nucleotide binding and/or hydrolysis are clearly not required for ring formation.
DDC: 540 Chemie
540 Chemistry and allied sciences
570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 09 Chemie, Pharmazie u. Geowissensch.
Place: Mainz
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY-NC-ND
Information on rights of use:
Journal: FEBS letters
Pages or article number: 1876
Publisher: Wiley
Publisher place: Chichester
Issue date: 2021
ISSN: 1873-3468
Publisher DOI: 10.1002/1873-3468.14140
Appears in collections:JGU-Publikationen

Files in This Item:
  File Description SizeFormat
binding_andor_hydrolysis_of_p-20221017120017531.pdf1.39 MBAdobe PDFView/Open