6533b86ffe1ef96bd12cde81
RESEARCH PRODUCT
Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation
Carmen SiebenallerDirk SchneiderNadja HellmannLukas SchlösserMark HelmCarsten SachseCarsten SachseMartina C. Schmidt-denglerBenedikt JunglasBenedikt JunglasBenedikt JunglasDominik Jacobsubject
GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein Bindingdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-06-21 | FEBS Letters |