Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1991-8-2
pubmed:abstractText
Glutamine synthetase activity from Synechocystis sp. strain PCC 6803 is regulated as a function of the nitrogen source available in the medium. Addition of 0.25 mM NH4Cl to nitrate-grown cells promotes a clear short-term inactivation of glutamine synthetase, whose enzyme activity decreases to 5 to 10% of the initial value in 25 min. The intracellular levels of glutamine, determined under various conditions, taken together with the results obtained with azaserine (an inhibitor of transamidases), rule out the possibility that glutamine per se is responsible for glutamine synthetase inactivation. Nitrogen starvation attenuates the ammonium-mediated glutamine synthetase inactivation, indicating that glutamine synthetase regulation is modulated through the internal balance between carbon-nitrogen compounds and carbon compounds. The parallelism observed between the glutamine synthetase activity and the internal concentration of alpha-ketoglutarate suggests that this metabolite could play a role as a positive effector of glutamine synthetase activity in Synechocystis sp. Despite the similarities of this physiological system to that described for enterobacteria, the lack of in vivo 32P labeling of glutamine synthetase during the inactivation process excludes the existence of an adenylylation-deadenylylation system in this cyanobacterium.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-1967601, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-1973929, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2110911, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-238954, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2573289, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2865248, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2868840, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2874557, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-2908087, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-36043, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4144960, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4150122, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4150659, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-418057, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4399832, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4606417, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-4990298, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-5783887, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-6025412, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-6111293, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-6115380, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-6127334, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-811763, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-909432, http://linkedlifedata.com/resource/pubmed/commentcorrection/1676397-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
173
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4095-100
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Regulation of glutamine synthetase activity in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803 by the nitrogen source: effect of ammonium.
pubmed:affiliation
Departamento de Bioquímica Vegetal y Biología Molecular, Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't