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Phosphorylation of Type IA restriction-modification complex enzyme EcoKI on the HsdR subunit
Cajthamlová K, Sisáková E, Weiser J, Weiserová M.
Jazyk angličtina Země Velká Británie
NLK
ProQuest Central
od 1996-01-01 do 2012-12-31
Medline Complete (EBSCOhost)
od 2006-01-01 do 2014-12-15
Health & Medicine (ProQuest)
od 1996-01-01 do 2012-12-31
Wiley Online Library (archiv)
od 1997-01-01 do 2012-12-31
Public Health Database (ProQuest)
od 1996-01-01 do 2012-12-31
Wiley Free Content
od 1997 do 2014
- MeSH
- chromatografie na tenké vrstvě MeSH
- elektroforéza MeSH
- Escherichia coli enzymologie metabolismus MeSH
- financování organizované MeSH
- fosfoaminokyseliny metabolismus MeSH
- fosforylace MeSH
- imunoprecipitace MeSH
- podjednotky proteinů metabolismus MeSH
- proteiny z Escherichia coli metabolismus MeSH
- restrikční endonukleasy typu I metabolismus MeSH
- restrikční enzymy metabolismus MeSH
- western blotting MeSH
Phosphorylation of Type I restriction-modification (R-M) enzymes EcoKI, EcoAI, and EcoR124I - representatives of IA, IB, and IC families, respectively - was analysed in vivo by immunoblotting of endogenous phosphoproteins isolated from Escherichia coli strains harbouring the corresponding hsd genes, and in vitro by a phosphorylation assay using protein kinase present in subcellular fractions of E. coli. From all three R-M enzymes, the HsdR subunit of EcoKI system was the only subunit that was phosphorylated. Further, evidence is presented that HsdR is phosphorylated in vivo only when coproduced with HsdM and HsdS subunits - as part of assembled EcoKI restriction endonuclease, while the individually produced HsdR subunit is not phosphorylated. In vitro phosphorylation of the HsdR subunit of purified EcoKI endonuclease occurs on Thr, and is strictly dependent on the addition of a catalytic amount of cytoplasmic fraction isolated from E. coli. So far this is the first case of phosphorylation of a Type I R-M enzyme reported.
Citace poskytuje Crossref.org
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- $a Phosphorylation of Type I restriction-modification (R-M) enzymes EcoKI, EcoAI, and EcoR124I - representatives of IA, IB, and IC families, respectively - was analysed in vivo by immunoblotting of endogenous phosphoproteins isolated from Escherichia coli strains harbouring the corresponding hsd genes, and in vitro by a phosphorylation assay using protein kinase present in subcellular fractions of E. coli. From all three R-M enzymes, the HsdR subunit of EcoKI system was the only subunit that was phosphorylated. Further, evidence is presented that HsdR is phosphorylated in vivo only when coproduced with HsdM and HsdS subunits - as part of assembled EcoKI restriction endonuclease, while the individually produced HsdR subunit is not phosphorylated. In vitro phosphorylation of the HsdR subunit of purified EcoKI endonuclease occurs on Thr, and is strictly dependent on the addition of a catalytic amount of cytoplasmic fraction isolated from E. coli. So far this is the first case of phosphorylation of a Type I R-M enzyme reported.
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