scholarly journals Site-directed mutagenesis of the temperature-sensing histidine protein kinase CorS from Pseudomonas syringae

2008 ◽  
Vol 283 (2) ◽  
pp. 231-238 ◽  
Author(s):  
Angela V. Smirnova ◽  
Yvonne Braun ◽  
Matthias S. Ullrich
Keyword(s):  
Protein Kinase ◽  
Pseudomonas Syringae ◽  
Temperature Sensing ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Histidine Protein Kinase

scholarly journals Residues in the Second Cysteine-rich Region of Protein Kinase C δ Relevant to Phorbol Ester Binding as Revealed by Site-directed Mutagenesis

1995 ◽  
Vol 270 (37) ◽  
pp. 21852-21859 ◽  
Author(s):  
Marcelo G. Kazanietz ◽  
Shaomeng Wang ◽  
George W. A. Milne ◽  
Nancy E. Lewin ◽  
Howard L. Liu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Rich Region ◽  
Kinase C

scholarly journals Phosphorylation of methylated-DNA–protein-cysteine S-methyltransferase at serine-204 significantly increases its resistance to proteolytic digestion

2000 ◽  
Vol 352 (3) ◽  
pp. 801-808
Author(s):  
In Kyoung LIM ◽  
Tae Jun PARK ◽  
Woon Ki PAIK
Keyword(s):  
Protein Kinase ◽  
Clin Oncol ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Proteolytic Digestion ◽  
Methylated Dna ◽  
Mgmt Protein ◽  
Rat Livers ◽  
Independent Protein

In a previous paper [Lim, Park, Jee, Lee and Paik (1999) J. Cancer Res. Clin. Oncol. 125, 493Ő499], we showed two major forms of active DNA-6-O-methylguanine:protein-L-cysteine S-methyltransferase (MGMT; EC 2.1.1.63) in the liver with N-nitrosodiethylamine (DEN)-induced carcinogenesis: these were 26 and 24kDa species. Here we show that a 2kDa C-terminal fragment was cleaved from the 26kDa species in vitro by thrombin or microsomal fractions isolated from DEN-treated rat livers. When Ser204 of the 26kDa protein was replaced with Ala by site-directed mutagenesis, phosphorylation of the protein was completely abolished, indicating Ser204 to be the site of phosphorylation. We also show that the phosphorylation was performed by Ca2+-independent protein kinase isoenzymes, and that the phosphorylated rat MGMT protein was resistant to digestion by protease(s) whose activity was increased during DEN-induced hepatocarcinogenesis and also by digestion with endopeptidase Glu-C (V8 protease).

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