Loading…
Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae
The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature Fae...
Saved in:
Published in: | Journal of bacteriology 1992-01, Vol.174 (20), p.6350-6358 |
---|---|
Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | |
container_end_page | 6358 |
container_issue | 20 |
container_start_page | 6350 |
container_title | Journal of bacteriology |
container_volume | 174 |
creator | Bakker, D Willemsen, PTJ Willems, R H Huisman, T T Mooi, FR Oudega, B Stegehuis, F de Graaf, FK |
description | The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature FaeF, FaeH, FaeI, and FaeJ proteins were calculated to be 15,161, 25,461, 24,804, and 25,093 Da, respectively. FaeH, FaeI, and FaeJ showed significant homology with FaeG, the major fimbrial subunit of K88 fimbriae. Mutations in the respective genes were constructed. Analysis of the mutants showed that the minor fimbrial subunits FaeF and FaeH play an essential role in the biogenesis but not in the adhesive properties of the K88 fimbriae. Mutations in faeI or faeJ had no significant effect on K88 production or adhesive capacity. Immunoblotting and immunoelectron microscopy revealed that FaeF and FaeH are located in or along the K88 fimbrial structure. |
format | article |
fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_16309863</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16309863</sourcerecordid><originalsourceid>FETCH-proquest_miscellaneous_163098633</originalsourceid><addsrcrecordid>eNqNiz0LwjAUADMoWD_-Qya3QtLU0s6iKI66l7RN8En6on1JwX-vgu5Od8PdhCVCZDKtZKVmbE50E0Lm-SZL2PnYGQxgodUBPHJveQ_oB26hbwbQ6DjFJiIE4oCjd6Pp3sIb8PTEcDUE9JlOZflbzJJNrXZkVl8u2Hq_u2wP6X3wj2go1D1Qa5zTaHykWhZKVGWh1N_hC7h5Qxk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16309863</pqid></control><display><type>article</type><title>Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae</title><source>PubMed (Medline)</source><source>American Society for Microbiology Journals</source><creator>Bakker, D ; Willemsen, PTJ ; Willems, R H ; Huisman, T T ; Mooi, FR ; Oudega, B ; Stegehuis, F ; de Graaf, FK</creator><creatorcontrib>Bakker, D ; Willemsen, PTJ ; Willems, R H ; Huisman, T T ; Mooi, FR ; Oudega, B ; Stegehuis, F ; de Graaf, FK</creatorcontrib><description>The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature FaeF, FaeH, FaeI, and FaeJ proteins were calculated to be 15,161, 25,461, 24,804, and 25,093 Da, respectively. FaeH, FaeI, and FaeJ showed significant homology with FaeG, the major fimbrial subunit of K88 fimbriae. Mutations in the respective genes were constructed. Analysis of the mutants showed that the minor fimbrial subunits FaeF and FaeH play an essential role in the biogenesis but not in the adhesive properties of the K88 fimbriae. Mutations in faeI or faeJ had no significant effect on K88 production or adhesive capacity. Immunoblotting and immunoelectron microscopy revealed that FaeF and FaeH are located in or along the K88 fimbrial structure.</description><identifier>ISSN: 0021-9193</identifier><language>eng</language><subject>Escherichia coli</subject><ispartof>Journal of bacteriology, 1992-01, Vol.174 (20), p.6350-6358</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>Bakker, D</creatorcontrib><creatorcontrib>Willemsen, PTJ</creatorcontrib><creatorcontrib>Willems, R H</creatorcontrib><creatorcontrib>Huisman, T T</creatorcontrib><creatorcontrib>Mooi, FR</creatorcontrib><creatorcontrib>Oudega, B</creatorcontrib><creatorcontrib>Stegehuis, F</creatorcontrib><creatorcontrib>de Graaf, FK</creatorcontrib><title>Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae</title><title>Journal of bacteriology</title><description>The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature FaeF, FaeH, FaeI, and FaeJ proteins were calculated to be 15,161, 25,461, 24,804, and 25,093 Da, respectively. FaeH, FaeI, and FaeJ showed significant homology with FaeG, the major fimbrial subunit of K88 fimbriae. Mutations in the respective genes were constructed. Analysis of the mutants showed that the minor fimbrial subunits FaeF and FaeH play an essential role in the biogenesis but not in the adhesive properties of the K88 fimbriae. Mutations in faeI or faeJ had no significant effect on K88 production or adhesive capacity. Immunoblotting and immunoelectron microscopy revealed that FaeF and FaeH are located in or along the K88 fimbrial structure.</description><subject>Escherichia coli</subject><issn>0021-9193</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqNiz0LwjAUADMoWD_-Qya3QtLU0s6iKI66l7RN8En6on1JwX-vgu5Od8PdhCVCZDKtZKVmbE50E0Lm-SZL2PnYGQxgodUBPHJveQ_oB26hbwbQ6DjFJiIE4oCjd6Pp3sIb8PTEcDUE9JlOZflbzJJNrXZkVl8u2Hq_u2wP6X3wj2go1D1Qa5zTaHykWhZKVGWh1N_hC7h5Qxk</recordid><startdate>19920101</startdate><enddate>19920101</enddate><creator>Bakker, D</creator><creator>Willemsen, PTJ</creator><creator>Willems, R H</creator><creator>Huisman, T T</creator><creator>Mooi, FR</creator><creator>Oudega, B</creator><creator>Stegehuis, F</creator><creator>de Graaf, FK</creator><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19920101</creationdate><title>Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae</title><author>Bakker, D ; Willemsen, PTJ ; Willems, R H ; Huisman, T T ; Mooi, FR ; Oudega, B ; Stegehuis, F ; de Graaf, FK</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_163098633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Escherichia coli</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bakker, D</creatorcontrib><creatorcontrib>Willemsen, PTJ</creatorcontrib><creatorcontrib>Willems, R H</creatorcontrib><creatorcontrib>Huisman, T T</creatorcontrib><creatorcontrib>Mooi, FR</creatorcontrib><creatorcontrib>Oudega, B</creatorcontrib><creatorcontrib>Stegehuis, F</creatorcontrib><creatorcontrib>de Graaf, FK</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bakker, D</au><au>Willemsen, PTJ</au><au>Willems, R H</au><au>Huisman, T T</au><au>Mooi, FR</au><au>Oudega, B</au><au>Stegehuis, F</au><au>de Graaf, FK</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae</atitle><jtitle>Journal of bacteriology</jtitle><date>1992-01-01</date><risdate>1992</risdate><volume>174</volume><issue>20</issue><spage>6350</spage><epage>6358</epage><pages>6350-6358</pages><issn>0021-9193</issn><abstract>The nucleotide sequences of the genes faeF, faeH, faeI, and faeJ encoding K88 minor fimbrial subunits were determined. Analysis of the primary structure of the gene products revealed that all four proteins are synthesized with an amino-terminal signal sequence. The molecular masses of the mature FaeF, FaeH, FaeI, and FaeJ proteins were calculated to be 15,161, 25,461, 24,804, and 25,093 Da, respectively. FaeH, FaeI, and FaeJ showed significant homology with FaeG, the major fimbrial subunit of K88 fimbriae. Mutations in the respective genes were constructed. Analysis of the mutants showed that the minor fimbrial subunits FaeF and FaeH play an essential role in the biogenesis but not in the adhesive properties of the K88 fimbriae. Mutations in faeI or faeJ had no significant effect on K88 production or adhesive capacity. Immunoblotting and immunoelectron microscopy revealed that FaeF and FaeH are located in or along the K88 fimbrial structure.</abstract></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9193 |
ispartof | Journal of bacteriology, 1992-01, Vol.174 (20), p.6350-6358 |
issn | 0021-9193 |
language | eng |
recordid | cdi_proquest_miscellaneous_16309863 |
source | PubMed (Medline); American Society for Microbiology Journals |
subjects | Escherichia coli |
title | Identification of minor fimbrianl subunits involved in biosynthesis of K88 fimbriae |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T08%3A05%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20minor%20fimbrianl%20subunits%20involved%20in%20biosynthesis%20of%20K88%20fimbriae&rft.jtitle=Journal%20of%20bacteriology&rft.au=Bakker,%20D&rft.date=1992-01-01&rft.volume=174&rft.issue=20&rft.spage=6350&rft.epage=6358&rft.pages=6350-6358&rft.issn=0021-9193&rft_id=info:doi/&rft_dat=%3Cproquest%3E16309863%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-proquest_miscellaneous_163098633%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=16309863&rft_id=info:pmid/&rfr_iscdi=true |