Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803

被引:74
作者
Hisbergues, M
Jeanjean, R
Joset, F
de Marsac, NT
Bédu, S
机构
[1] CNRS, Chim Bacterienne Lab, F-13402 Marseille 20, France
[2] Inst Pasteur, Unite Physiol Microbienne, F-75724 Paris 15, France
来源
FEBS LETTERS | 1999年 / 463卷 / 03期
关键词
protein PII; cyanobacterium; nitrate uptake; bicarbonate uptake; phosphorylation; redox state;
D O I
10.1016/S0014-5793(99)01624-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In Synechocystis PCC 6803 as in other cyanobacteria. involvement of protein PII in the co-regulation of inorganic carbon and nitrogen metabolism was established based on posttranslational modifications of the protein resulting from changes in the carbon/nitrogen regimes. Uptake of bicarbonate and nitrate in response to changes of the carbon and/or nitrogen regimes is altered in a PII-null. mutant, indicating that both processes are under control of PII. Modulation of electron flow by addition of methyl viologen with or without duroquinol, or in a NAD(P)H dehydrogenase-deficient mutant, affects the phosphorylation level of PII. The redox state of the cells would thus act as a trigger for PII phosphorylation. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:216 / 220
页数:5
相关论文
共 25 条
[1]   PROTEIN-PHOSPHORYLATION IN REGULATION OF PHOTOSYNTHESIS [J].
ALLEN, JF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1098 (03) :275-335
[2]   UPTAKE OF INORGANIC CARBON IN THE CYANOBACTERIUM SYNECHOCYSTIS PCC6803 - PHYSIOLOGICAL AND GENETIC-EVIDENCE FOR A HIGH-AFFINITY UPTAKE SYSTEM [J].
BEDU, S ;
POZUELOS, P ;
CAMI, B ;
JOSET, F .
MOLECULAR MICROBIOLOGY, 1995, 18 (03) :559-568
[3]   Phosphoprotein P-II from cyanobacteria - Analysis of functional conservation with the P-II signal-transduction protein from Escherichia coli [J].
Forchhammer, K ;
Hedler, A .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 244 (03) :869-875
[4]   PHOSPHORYLATION OF THE P-II PROTEIN (GLNB GENE-PRODUCT) IN THE CYANOBACTERIUM SYNECHOCOCCUS SP STRAIN PCC-7942 - ANALYSIS OF IN-VITRO KINASE-ACTIVITY [J].
FORCHHAMMER, K ;
DEMARSAC, NT .
JOURNAL OF BACTERIOLOGY, 1995, 177 (20) :5812-5817
[5]   FUNCTIONAL-ANALYSIS OF THE PHOSPHOPROTEIN P-II (GLNB GENE-PRODUCT) IN THE CYANOBACTERIUM SYNECHOCOCCUS SP STRAIN PCC-7942 [J].
FORCHHAMMER, K ;
DEMARSAC, NT .
JOURNAL OF BACTERIOLOGY, 1995, 177 (08) :2033-2040
[6]   THE P-II PROTEIN IN THE CYANOBACTERIUM SYNECHOCOCCUS SP STRAIN PCC-7942 IS MODIFIED BY SERINE PHOSPHORYLATION AND SIGNALS THE CELLULAR N-STATUS [J].
FORCHHAMMER, K ;
DEMARSAC, NT .
JOURNAL OF BACTERIOLOGY, 1994, 176 (01) :84-91
[7]   Redox-controlled thylakoid protein phosphorylation. News and views [J].
Gal, A ;
Zer, H ;
Ohad, I .
PHYSIOLOGIA PLANTARUM, 1997, 100 (04) :869-885
[8]   Nitrogen availability and electron transport control the expression of glnB gene (encoding PII protein) in the cyanobacterium Synechocystis sp. PCC 6803 [J].
García-Domínguez, M ;
Florencio, FJ .
PLANT MOLECULAR BIOLOGY, 1997, 35 (06) :723-734
[9]   MODIFICATION OF A GLNB-LIKE GENE-PRODUCT BY PHOTOSYNTHETIC ELECTRON-TRANSPORT IN THE CYANOBACTERIUM-SYNECHOCOCCUS 6301 [J].
HARRISON, MA ;
KEEN, JN ;
FINDLAY, JBC ;
ALLEN, JF .
FEBS LETTERS, 1990, 264 (01) :25-28
[10]   Dephosphorylation of the phosphoprotein P-II in Synechococcus PCC 7942: identification of an ATP and 2-oxoglutarate-regulated phosphatase activity [J].
Irmler, A ;
Sanner, S ;
Dierks, H ;
Forchhammer, K .
MOLECULAR MICROBIOLOGY, 1997, 26 (01) :81-90