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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
The Leptospira interrogans ponA and pbpB genes were isolated and characterized. ponA and pbpB encode the penicillin-binding proteins (PBPs) 1 and 3, respectively. There is little sequence variation between the PBP genes from two L. interrogans strains (serovar icterohaemorrhagiae strain Verdun and serovar pomona strain RZ11). The deduced L. interrogans PBP 1 and PBP 3 protein sequences from the two strains shared over 50% similarity to homologous proteins from Escherichia coli. It was demonstrated for strain Verdun that ponA and pbpB are transcribed individually from their own promoter. The ponA and pbpB genes from both strains are separated by 8 to 10 kb and oriented such that their transcription is convergent. The L. interrogans PBP 1 and PBP 3 proteins were synthesized in E. coli and were modified with ampicillin using a digoxigenin-ampicillin conjugate. These data show that both genes encode functional PBPs.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-10027275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-10620683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-10878114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-14266934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-1656379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-1741619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-1997416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-319999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-3243435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-5219821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-6027998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-6259125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-6660857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-6947280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-8192459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-8491705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9228761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9254694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9404617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9440513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9449253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9588807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11181373-9614966
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsI protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide...,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan Glycosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
870-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11181373-Adenosine Monophosphate,
pubmed-meshheading:11181373-Amino Acid Sequence,
pubmed-meshheading:11181373-Bacterial Proteins,
pubmed-meshheading:11181373-Carrier Proteins,
pubmed-meshheading:11181373-DNA Primers,
pubmed-meshheading:11181373-Escherichia coli Proteins,
pubmed-meshheading:11181373-Hexosyltransferases,
pubmed-meshheading:11181373-Leptospira interrogans,
pubmed-meshheading:11181373-Molecular Weight,
pubmed-meshheading:11181373-Multienzyme Complexes,
pubmed-meshheading:11181373-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:11181373-Penicillin-Binding Proteins,
pubmed-meshheading:11181373-Penicillins,
pubmed-meshheading:11181373-Peptidoglycan Glycosyltransferase,
pubmed-meshheading:11181373-Peptidyl Transferases,
pubmed-meshheading:11181373-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11181373-Sequence Homology, Amino Acid,
pubmed-meshheading:11181373-Serotyping,
pubmed-meshheading:11181373-Transcription, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
Penicillin-binding proteins in Leptospira interrogans.
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pubmed:affiliation |
Unité de Bactériologie Moléculaire et Médicale, Institut Pasteur, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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