Orientation of the peptidoglycan chains in the sacculus of Escherichia coli
The organization of chains of oligopeptidoglycan in the saccular wall is of critical importance in the study of the mechanism and physiology of prokaryotic wall growth. The electron microphotographs of De Pedro et al, present new findings and can be used to negate or at least raise questions about t...
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Veröffentlicht in: | Research in microbiology 1998-11, Vol.149 (10), p.689-701 |
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description | The organization of chains of oligopeptidoglycan in the saccular wall is of critical importance in the study of the mechanism and physiology of prokaryotic wall growth. The electron microphotographs of De Pedro
et al, present new findings and can be used to negate or at least raise questions about the previously accepted conclusion that the glycan chains are oriented transversely to the axis of rod-shaped
Escherichia coli. This suggests caution in assuming that the glycan chains in the murein structure are parallel to each other and are perpendicular to the axis of the cell.
These results should reopen the question of not only the orientation of the peptidoglycan chains, but the possibility of variability in orientation. Three classes of hypotheses about wall growth are reconsidered and problems with them are presented. The new results from De Pedro's laboratory and the experimental glycan chain length distribution argue against proposed systematic models. These include models that postulate belts or hoops stretched around the circumference of the cell and mechanisms that insert new chains of the length of presumptive “docking” strands in the stress-bearing wall. They are consistent, however, with the surface stress theory that proposes that random enzyme action together with physical forces are involved in the elongation of the rod-shaped Gram-negative wall. |
doi_str_mv | 10.1016/S0923-2508(99)80016-3 |
format | Article |
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et al, present new findings and can be used to negate or at least raise questions about the previously accepted conclusion that the glycan chains are oriented transversely to the axis of rod-shaped
Escherichia coli. This suggests caution in assuming that the glycan chains in the murein structure are parallel to each other and are perpendicular to the axis of the cell.
These results should reopen the question of not only the orientation of the peptidoglycan chains, but the possibility of variability in orientation. Three classes of hypotheses about wall growth are reconsidered and problems with them are presented. The new results from De Pedro's laboratory and the experimental glycan chain length distribution argue against proposed systematic models. These include models that postulate belts or hoops stretched around the circumference of the cell and mechanisms that insert new chains of the length of presumptive “docking” strands in the stress-bearing wall. They are consistent, however, with the surface stress theory that proposes that random enzyme action together with physical forces are involved in the elongation of the rod-shaped Gram-negative wall.</description><identifier>ISSN: 0923-2508</identifier><identifier>EISSN: 1769-7123</identifier><identifier>DOI: 10.1016/S0923-2508(99)80016-3</identifier><identifier>PMID: 9921576</identifier><language>eng</language><publisher>Paris: Elsevier SAS</publisher><subject>Bacteriology ; Biological and medical sciences ; Cell wall ; Cell Wall - chemistry ; Cell Wall - metabolism ; Chaînes de glycans ; Echerichia coli ; Elongation ; Escherichia coli ; Escherichia coli - chemistry ; Fundamental and applied biological sciences. Psychology ; Glycan chains ; Microbiology ; Models, Molecular ; Modèles ; Morphology, structure, chemical composition ; Murein ; Muréine ; Orientation ; Paroi cellulaire ; Peptidoglycan ; Peptidoglycan - biosynthesis ; Peptidoglycan - chemistry ; Review ; Revue ; Sacculus ; Tessera</subject><ispartof>Research in microbiology, 1998-11, Vol.149 (10), p.689-701</ispartof><rights>1998 Institut Pasteur/Elsevier</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-aa6e22c1c6a3f6a5e587bf495aa785cf11d0ad3b1374aa362a93157c44ba102f3</citedby><cites>FETCH-LOGICAL-c467t-aa6e22c1c6a3f6a5e587bf495aa785cf11d0ad3b1374aa362a93157c44ba102f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0923-2508(99)80016-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1661226$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9921576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koch, A.L.</creatorcontrib><title>Orientation of the peptidoglycan chains in the sacculus of Escherichia coli</title><title>Research in microbiology</title><addtitle>Res Microbiol</addtitle><description>The organization of chains of oligopeptidoglycan in the saccular wall is of critical importance in the study of the mechanism and physiology of prokaryotic wall growth. The electron microphotographs of De Pedro
et al, present new findings and can be used to negate or at least raise questions about the previously accepted conclusion that the glycan chains are oriented transversely to the axis of rod-shaped
Escherichia coli. This suggests caution in assuming that the glycan chains in the murein structure are parallel to each other and are perpendicular to the axis of the cell.
These results should reopen the question of not only the orientation of the peptidoglycan chains, but the possibility of variability in orientation. Three classes of hypotheses about wall growth are reconsidered and problems with them are presented. The new results from De Pedro's laboratory and the experimental glycan chain length distribution argue against proposed systematic models. These include models that postulate belts or hoops stretched around the circumference of the cell and mechanisms that insert new chains of the length of presumptive “docking” strands in the stress-bearing wall. They are consistent, however, with the surface stress theory that proposes that random enzyme action together with physical forces are involved in the elongation of the rod-shaped Gram-negative wall.</description><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cell wall</subject><subject>Cell Wall - chemistry</subject><subject>Cell Wall - metabolism</subject><subject>Chaînes de glycans</subject><subject>Echerichia coli</subject><subject>Elongation</subject><subject>Escherichia coli</subject><subject>Escherichia coli - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycan chains</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Modèles</subject><subject>Morphology, structure, chemical composition</subject><subject>Murein</subject><subject>Muréine</subject><subject>Orientation</subject><subject>Paroi cellulaire</subject><subject>Peptidoglycan</subject><subject>Peptidoglycan - biosynthesis</subject><subject>Peptidoglycan - chemistry</subject><subject>Review</subject><subject>Revue</subject><subject>Sacculus</subject><subject>Tessera</subject><issn>0923-2508</issn><issn>1769-7123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LwzAYx4MoOl8-wqAHET1Um6RJmpPI8A0HHtRzePY0dZGunUkr7NubbmMePSXk_3te-IWQMc2uaUblzVumGU-ZyIpLra-KLL6lfI-MqJI6VZTxfTLaIUfkOISvyAil8kNyqDWLVzkiL6_e2aaDzrVN0lZJN7fJ0i47V7af9QqhSXAOrgmJa9ZZAMS-7sPA3gecW-9w7iDBtnan5KCCOtiz7XlCPh7u3ydP6fT18XlyN00xl6pLAaRlDClK4JUEYUWhZlWuBYAqBFaUlhmUfEa5ygG4ZKB5XBbzfAY0YxU_IRebvkvffvc2dGbhAtq6hsa2fTBS01znQvwLUsUKVfAigmIDom9D8LYyS-8W4FeGZmawbda2zaDSaG3Wtg2PdePtgH62sOWuaqs35ufbHAJCXXlo0IW_5lJSxgbsdoPZaO3HWW8Cxl9BWzpvsTNl6_5Z5BeWpZtk</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Koch, A.L.</creator><general>Elsevier SAS</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Orientation of the peptidoglycan chains in the sacculus of Escherichia coli</title><author>Koch, A.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c467t-aa6e22c1c6a3f6a5e587bf495aa785cf11d0ad3b1374aa362a93157c44ba102f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cell wall</topic><topic>Cell Wall - chemistry</topic><topic>Cell Wall - metabolism</topic><topic>Chaînes de glycans</topic><topic>Echerichia coli</topic><topic>Elongation</topic><topic>Escherichia coli</topic><topic>Escherichia coli - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycan chains</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Modèles</topic><topic>Morphology, structure, chemical composition</topic><topic>Murein</topic><topic>Muréine</topic><topic>Orientation</topic><topic>Paroi cellulaire</topic><topic>Peptidoglycan</topic><topic>Peptidoglycan - biosynthesis</topic><topic>Peptidoglycan - chemistry</topic><topic>Review</topic><topic>Revue</topic><topic>Sacculus</topic><topic>Tessera</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koch, A.L.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Research in microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koch, A.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Orientation of the peptidoglycan chains in the sacculus of Escherichia coli</atitle><jtitle>Research in microbiology</jtitle><addtitle>Res Microbiol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>149</volume><issue>10</issue><spage>689</spage><epage>701</epage><pages>689-701</pages><issn>0923-2508</issn><eissn>1769-7123</eissn><abstract>The organization of chains of oligopeptidoglycan in the saccular wall is of critical importance in the study of the mechanism and physiology of prokaryotic wall growth. The electron microphotographs of De Pedro
et al, present new findings and can be used to negate or at least raise questions about the previously accepted conclusion that the glycan chains are oriented transversely to the axis of rod-shaped
Escherichia coli. This suggests caution in assuming that the glycan chains in the murein structure are parallel to each other and are perpendicular to the axis of the cell.
These results should reopen the question of not only the orientation of the peptidoglycan chains, but the possibility of variability in orientation. Three classes of hypotheses about wall growth are reconsidered and problems with them are presented. The new results from De Pedro's laboratory and the experimental glycan chain length distribution argue against proposed systematic models. These include models that postulate belts or hoops stretched around the circumference of the cell and mechanisms that insert new chains of the length of presumptive “docking” strands in the stress-bearing wall. They are consistent, however, with the surface stress theory that proposes that random enzyme action together with physical forces are involved in the elongation of the rod-shaped Gram-negative wall.</abstract><cop>Paris</cop><pub>Elsevier SAS</pub><pmid>9921576</pmid><doi>10.1016/S0923-2508(99)80016-3</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Access via ScienceDirect (Elsevier) |
subjects | Bacteriology Biological and medical sciences Cell wall Cell Wall - chemistry Cell Wall - metabolism Chaînes de glycans Echerichia coli Elongation Escherichia coli Escherichia coli - chemistry Fundamental and applied biological sciences. Psychology Glycan chains Microbiology Models, Molecular Modèles Morphology, structure, chemical composition Murein Muréine Orientation Paroi cellulaire Peptidoglycan Peptidoglycan - biosynthesis Peptidoglycan - chemistry Review Revue Sacculus Tessera |
title | Orientation of the peptidoglycan chains in the sacculus of Escherichia coli |
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