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@ARTICLE{Siebenaller:903528,
author = {Siebenaller, Carmen and Schlösser, Lukas and Junglas,
Benedikt and Schmidt-Dengler, Martina and Jacob, Dominik and
Hellmann, Nadja and Sachse, Carsten and Helm, Mark and
Schneider, Dirk},
title = {{B}inding and/or hydrolysis of purine‐based nucleotides
is not required for {IM}30 ring formation},
journal = {FEBS letters},
volume = {595},
number = {14},
issn = {0014-5793},
address = {Chichester},
publisher = {Wiley},
reportid = {FZJ-2021-05196},
pages = {1876 - 1885},
year = {2021},
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.},
cin = {ER-C-3},
ddc = {610},
cid = {I:(DE-Juel1)ER-C-3-20170113},
pnm = {5352 - Understanding the Functionality of Soft Matter and
Biomolecular Systems (POF4-535)},
pid = {G:(DE-HGF)POF4-5352},
typ = {PUB:(DE-HGF)16},
pubmed = {34060653},
UT = {WOS:000663865600001},
doi = {10.1002/1873-3468.14140},
url = {https://juser.fz-juelich.de/record/903528},
}