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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-10-8
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pubmed:abstractText |
Permeabilization with cetyl trimethyl ammonium bromide was used to study the post-translational modification of the PII protein in Rhizobium leguminosarum. Upon incubation with radioactive UTP a single band was obtained after SDS-PAGE and autoradiography. RNase resistance and snake venom phosphodiesterase sensitivity showed that radioactivity was bound through a phosphodiester bond to a protein which was absorbed by an antiserum specific for the PII protein. Uridylylation of the PII protein was shown to be dependent on the modifications of the glutamine/alpha-ketoglutarate ratio.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
330
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pubmed:geneSymbol |
glnB,
kan
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8370467-Autoradiography,
pubmed-meshheading:8370467-Bacterial Proteins,
pubmed-meshheading:8370467-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8370467-Glutamine,
pubmed-meshheading:8370467-Ketoglutaric Acids,
pubmed-meshheading:8370467-PII Nitrogen Regulatory Proteins,
pubmed-meshheading:8370467-Protein Processing, Post-Translational,
pubmed-meshheading:8370467-Rhizobium leguminosarum,
pubmed-meshheading:8370467-Uridine,
pubmed-meshheading:8370467-Uridine Triphosphate
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pubmed:year |
1993
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pubmed:articleTitle |
Uridylylation of the PII protein in Rhizobium leguminosarum.
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pubmed:affiliation |
International Institute of Genetics and Biophysics, Naples, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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