The penicillin-binding proteins of Caulobacter crescentus

The proteins that specifically bind penicillin G were studied with Caulobacter crescentus. This organism possessed at least 5 penicillin-binding proteins (PBPs): PBP 1A (132 K), PBP 1Bs (98 K), PBP 2 (77 K), PBP 3 (64 K), and PBP 4 (50 K). As expected from the unique morphology, the C. crescentus PB...

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Bibliographic Details
Published inJournal of biochemistry (Tokyo) Vol. 87; no. 1; pp. 363 - 366
Main Authors KOYASU, Shigeo, FUKUDA, Akio, OKADA, Yoshimi
Format Journal Article
LanguageEnglish
Published England Oxford University Press 1980
Subjects
Bacteria - analysis
Bacterial Proteins
Carrier Proteins - isolation & purification
Cell Membrane - analysis
Escherichia coli - analysis
Hexosyltransferases
Membrane Proteins - isolation & purification
Molecular Weight
Muramoylpentapeptide Carboxypeptidase
Penicillin G
Penicillin-Binding Proteins
Penicillins - isolation & purification
Peptidyl Transferases
Species Specificity
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Summary:The proteins that specifically bind penicillin G were studied with Caulobacter crescentus. This organism possessed at least 5 penicillin-binding proteins (PBPs): PBP 1A (132 K), PBP 1Bs (98 K), PBP 2 (77 K), PBP 3 (64 K), and PBP 4 (50 K). As expected from the unique morphology, the C. crescentus PBPs were different from those of other sources in molecular weight and localization: C. crescentus did not possess PBPs of low molecular weight. PBP 4 was found only in the outer membrane, while the other PBPs were present mostly in the inner membrane.
Bibliography:F60
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ark:/67375/HXZ-RGNJBRXC-7
istex:D0F8BB8826D7783855D0A968158B30F65C0644EB
1 This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan.
ArticleID:87.1.363
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a132749