دورية أكاديمية
Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: attachment of long-chain fatty acids to escherichia coli peptidoglycan.
| العنوان: | Intraperiplasmic growth of Bdellovibrio bacteriovorus 109J: attachment of long-chain fatty acids to escherichia coli peptidoglycan. |
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| المؤلفون: | Thomashow MF, Rittenberg SC |
| المصدر: | Journal of bacteriology [J Bacteriol] 1978 Sep; Vol. 135 (3), pp. 1015-23. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Print Cited Medium: Print ISSN: 0021-9193 (Print) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, DC : American Society for Microbiology |
| مواضيع طبية MeSH: | Escherichia coli*, Bdellovibrio/*metabolism , Fatty Acids/*metabolism , Peptidoglycan/*metabolism, Acylation ; Bdellovibrio/growth & development ; Models, Biological ; Oleic Acids/metabolism ; Palmitic Acids/metabolism |
| مستخلص: | During the initial stages of intraperiplasmic growth of Bdellovibrio bacteriovorus on Escherichia coli, the peptidoglycan of the E. coli becomes acylated with long-chain fatty acids, primarily palmitic acid (60%) and oleic acid (20%). The attachment of the fatty acids to the peptidoglycan involves a carboxylic-ester bond, i.e., they were removed by treatment with alkaline hydroxylamine. Their linkage to the peptidoglycan does not involve a protein molecule. When the bdelloplast peptidoglycan was digested with lysozyme, the fatty acid-containing split products behaved as lipopeptidoglycan, i.e., they were extracted into the organic phase of 1-butanol:acetic acid:water (4:15) two-phase system; all of the lysozyme split products generated from normal E. coli peptidoglycan were extracted into the water phase. It is suggested that the function of the acylation reaction is to help stabilize the bdelloplast outer membrane against osmotic forces. In addition, a model is presented to explain how a bdellovibrio penetrates, stabilizes, and lyses a substrate cell. |
| References: | Biochim Biophys Acta. 1959 Jul;34:244-5. (PMID: 13832326) J Bacteriol. 1978 Sep;135(3):1008-14. (PMID: 357410) J Bacteriol. 1978 Mar;133(3):1484-91. (PMID: 641013) J Bacteriol. 1974 May;118(2):663-80. (PMID: 4208138) Bacteriol Rev. 1972 Dec;36(4):407-77. (PMID: 4568761) J Bacteriol. 1972 Sep;111(3):664-73. (PMID: 4559819) Eur J Biochem. 1972 Jul 13;28(2):166-73. (PMID: 5069711) Biochem Biophys Res Commun. 1969 Oct 22;37(3):518-25. (PMID: 4900142) Eur J Biochem. 1969 Oct;10(3):426-38. (PMID: 4899922) J Bacteriol. 1966 May;91(5):2006-17. (PMID: 5327913) J Bacteriol. 1975 Mar;121(3):1158-65. (PMID: 1090596) J Bacteriol. 1975 Mar;121(3):1145-57. (PMID: 1090595) J Bacteriol. 1975 Mar;121(3):1137-44. (PMID: 1090594) J Bacteriol. 1975 Aug;123(2):481-91. (PMID: 1097411) |
| المشرفين على المادة: | 0 (Fatty Acids) 0 (Oleic Acids) 0 (Palmitic Acids) 0 (Peptidoglycan) |
| تواريخ الأحداث: | Date Created: 19780901 Date Completed: 19781129 Latest Revision: 20210526 |
| رمز التحديث: | 20240627 |
| مُعرف محوري في PubMed: | PMC222478 |
| DOI: | 10.1128/jb.135.3.1015-1023.1978 |
| PMID: | 357411 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9193 |
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| DOI: | 10.1128/jb.135.3.1015-1023.1978 |