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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 |
1999-2-5
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pubmed:databankReference |
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pubmed:abstractText |
A 4.2-kb SphI-BamHI fragment of chromosomal DNA from Streptomyces granaticolor was cloned and shown to encode a protein with significant sequence similarity to the eukaryotic protein serine/threonine kinases. It consists of 701 amino acids and in the N-terminal part contains all conserved catalytic domains of protein kinases. The C-terminal domain of Pkg2 contains seven tandem repeats of 11 or 12 amino acids with similarity to the tryptophan-docking motif known to stabilize a symmetrical three-dimensional structure called a propeller structure. The pkg2 gene was overexpressed in Escherichia coli, and the gene product (Pkg2) has been found to be autophosphorylated at serine and threonine residues. The N- and C-terminal parts of Pkg2 are separated with a hydrophobic stretch of 21 amino acids which translocated a PhoA fusion protein into the periplasm. Thus, Pkg2 is the first transmembrane protein serine/threonine kinase described for streptomycetes. Replacement of the pkg2 gene by the spectinomycin resistance gene resulted in changes in the morphology of aerial hyphae.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-1100846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-1835671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2199796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2540676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2556636,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2792083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-2999794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-3162770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-3291115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-3860846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-6096212,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-6843658,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-7735834,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-9197550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-9278503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-9573144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-9613569,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/9864307-9799102
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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 |
Jan
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-23
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9864307-Amino Acid Sequence,
pubmed-meshheading:9864307-Base Sequence,
pubmed-meshheading:9864307-Cloning, Molecular,
pubmed-meshheading:9864307-DNA, Bacterial,
pubmed-meshheading:9864307-DNA Primers,
pubmed-meshheading:9864307-Escherichia coli,
pubmed-meshheading:9864307-Gene Expression,
pubmed-meshheading:9864307-Genes, Bacterial,
pubmed-meshheading:9864307-Microscopy, Electron, Scanning,
pubmed-meshheading:9864307-Molecular Sequence Data,
pubmed-meshheading:9864307-Mutation,
pubmed-meshheading:9864307-Phenotype,
pubmed-meshheading:9864307-Phosphorylation,
pubmed-meshheading:9864307-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9864307-Recombinant Fusion Proteins,
pubmed-meshheading:9864307-Restriction Mapping,
pubmed-meshheading:9864307-Sequence Homology, Amino Acid,
pubmed-meshheading:9864307-Streptomyces
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pubmed:year |
1999
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pubmed:articleTitle |
Pkg2, a novel transmembrane protein Ser/Thr kinase of Streptomyces granaticolor.
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pubmed:affiliation |
Cell and Molecular Microbiology Division, Institute of Microbiology, Czech Academy of Sciences, 142 20 Prague 4, Czech Republic.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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