Journal Article

FZJ-2021-05196

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

Siebenaller, C. (Corresponding author) ; Schlösser, L. ; Junglas, B.FZJ* ; Schmidt-Dengler, M. ; Jacob, D. ; Hellmann, N. ; Sachse, C.FZJ* ; Helm, M. ; Schneider, D.

2021
Wiley Chichester

This record in other databases:      

Please use a persistent id in citations: http://hdl.handle.net/2128/31852  doi:10.1002/1873-3468.14140

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.

---

Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)

Appears in the scientific report 2021

---

Database coverage:
; ; ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

---