Removal of Mn2+ induces dissociation of glutamine synthetase fromStreptomyces aureofaciens

Autor:	V. Běhal, Kien Trung Nguyen, J. Kopecký, Lieu Thi Nguyen
Rok vydání:	1997
Předmět:	inorganic chemicals chemistry.chemical_classification biology Chemistry Protein subunit Streptomyces aureofaciens Fast protein liquid chromatography General Medicine Metabolism biology.organism_classification Microbiology Protein tertiary structure Divalent Enzyme Biochemistry Glutamine synthetase
Zdroj:	Folia Microbiologica. 42:539-543
ISSN:	1874-9356 0015-5632
DOI:	10.1007/bf02815461
Popis:	Removal of Mn2+ by EDTA treatment converted dodecameric glutamine synthetase (GS) fromStreptomyces aureofaciens into inactive subunits but did not affect significantly their conformation. However, when fractionated by gel filtration FPLC, the Mn2+-free subunits showed a 7-fold increase ofA280, probably due to a significant alteration in their tertiary structure. Mn2+ reduced theA280 of the subunits and promoted their reaggregation to form active GS. Mg2+ or Ca2+ but not Co2+ or Zn2+ might have similar effects. The results suggest that specific divalent cations might play a crucial role in stabilizing subunit interactions as well as the conformation of the individual subunits inStreptomyces GS. The role of specific divalent cations in the regulation of GS turnover is discussed.
Databáze:	OpenAIRE
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