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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Research in microbiology 1998-11, Vol.149 (10), p.689-701
1. Verfasser: Koch, A.L.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 701
container_issue 10
container_start_page 689
container_title Research in microbiology
container_volume 149
creator Koch, A.L.
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
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69149455</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0923250899800163</els_id><sourcerecordid>69149455</sourcerecordid><originalsourceid>FETCH-LOGICAL-c467t-aa6e22c1c6a3f6a5e587bf495aa785cf11d0ad3b1374aa362a93157c44ba102f3</originalsourceid><addsrcrecordid>eNqFkU1LwzAYx4MoOl8-wqAHET1Um6RJmpPI8A0HHtRzePY0dZGunUkr7NubbmMePSXk_3te-IWQMc2uaUblzVumGU-ZyIpLra-KLL6lfI-MqJI6VZTxfTLaIUfkOISvyAil8kNyqDWLVzkiL6_e2aaDzrVN0lZJN7fJ0i47V7af9QqhSXAOrgmJa9ZZAMS-7sPA3gecW-9w7iDBtnan5KCCOtiz7XlCPh7u3ydP6fT18XlyN00xl6pLAaRlDClK4JUEYUWhZlWuBYAqBFaUlhmUfEa5ygG4ZKB5XBbzfAY0YxU_IRebvkvffvc2dGbhAtq6hsa2fTBS01znQvwLUsUKVfAigmIDom9D8LYyS-8W4FeGZmawbda2zaDSaG3Wtg2PdePtgH62sOWuaqs35ufbHAJCXXlo0IW_5lJSxgbsdoPZaO3HWW8Cxl9BWzpvsTNl6_5Z5BeWpZtk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17287838</pqid></control><display><type>article</type><title>Orientation of the peptidoglycan chains in the sacculus of Escherichia coli</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Koch, A.L.</creator><creatorcontrib>Koch, A.L.</creatorcontrib><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><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>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=1661226$$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>
fulltext fulltext
identifier ISSN: 0923-2508
ispartof Research in microbiology, 1998-11, Vol.149 (10), p.689-701
issn 0923-2508
1769-7123
language eng
recordid cdi_proquest_miscellaneous_69149455
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T16%3A46%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Orientation%20of%20the%20peptidoglycan%20chains%20in%20the%20sacculus%20of%20Escherichia%20coli&rft.jtitle=Research%20in%20microbiology&rft.au=Koch,%20A.L.&rft.date=1998-11-01&rft.volume=149&rft.issue=10&rft.spage=689&rft.epage=701&rft.pages=689-701&rft.issn=0923-2508&rft.eissn=1769-7123&rft_id=info:doi/10.1016/S0923-2508(99)80016-3&rft_dat=%3Cproquest_cross%3E69149455%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17287838&rft_id=info:pmid/9921576&rft_els_id=S0923250899800163&rfr_iscdi=true