Characterization of BpH3, an H-NS-like protein in Bordetella pertussis
This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Goyard, Sophie [verfasserIn] Bertin, Philippe [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Oxford UK: Blackwell Science Ltd ; 1997 |
|---|
| Umfang: |
Online-Ressource |
|---|
| Reproduktion: |
2003 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 24(1997), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:24 ; year:1997 ; number:4 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1365-2958.1997.3891753.x |
|---|
| Katalog-ID: |
NLEJ243582749 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ243582749 | ||
| 003 | DE-627 | ||
| 005 | 20210707183036.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 120427s1997 xx |||||o 00| ||und c | ||
| 024 | 7 | |a 10.1046/j.1365-2958.1997.3891753.x |2 doi | |
| 035 | |a (DE-627)NLEJ243582749 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 100 | 1 | |a Goyard, Sophie |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| 264 | 1 | |a Oxford UK |b Blackwell Science Ltd |c 1997 | |
| 300 | |a Online-Ressource | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. | ||
| 533 | |d 2003 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2003|||||||||| | ||
| 700 | 1 | |a Bertin, Philippe |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i In |t Molecular microbiology |d Oxford [u.a.] : Wiley-Blackwell, 1987 |g 24(1997), 4, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243926537 |w (DE-600)1501537-3 |x 1365-2958 |7 nnns |
| 773 | 1 | 8 | |g volume:24 |g year:1997 |g number:4 |g pages:0 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-DJB | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 24 |j 1997 |e 4 |h 0 | ||
| author_variant |
s g sg p b pb |
|---|---|
| matchkey_str |
article:13652958:1997----::hrceiainfp3nnlkpoenno |
| hierarchy_sort_str |
1997 |
| publishDate |
1997 |
| allfields |
10.1046/j.1365-2958.1997.3891753.x doi (DE-627)NLEJ243582749 DE-627 ger DE-627 rakwb Goyard, Sophie verfasserin aut Characterization of BpH3, an H-NS-like protein in Bordetella pertussis Oxford UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Bertin, Philippe verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 24(1997), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:24 year:1997 number:4 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 24 1997 4 0 |
| spelling |
10.1046/j.1365-2958.1997.3891753.x doi (DE-627)NLEJ243582749 DE-627 ger DE-627 rakwb Goyard, Sophie verfasserin aut Characterization of BpH3, an H-NS-like protein in Bordetella pertussis Oxford UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Bertin, Philippe verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 24(1997), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:24 year:1997 number:4 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 24 1997 4 0 |
| allfields_unstemmed |
10.1046/j.1365-2958.1997.3891753.x doi (DE-627)NLEJ243582749 DE-627 ger DE-627 rakwb Goyard, Sophie verfasserin aut Characterization of BpH3, an H-NS-like protein in Bordetella pertussis Oxford UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Bertin, Philippe verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 24(1997), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:24 year:1997 number:4 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 24 1997 4 0 |
| allfieldsGer |
10.1046/j.1365-2958.1997.3891753.x doi (DE-627)NLEJ243582749 DE-627 ger DE-627 rakwb Goyard, Sophie verfasserin aut Characterization of BpH3, an H-NS-like protein in Bordetella pertussis Oxford UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Bertin, Philippe verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 24(1997), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:24 year:1997 number:4 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 24 1997 4 0 |
| allfieldsSound |
10.1046/j.1365-2958.1997.3891753.x doi (DE-627)NLEJ243582749 DE-627 ger DE-627 rakwb Goyard, Sophie verfasserin aut Characterization of BpH3, an H-NS-like protein in Bordetella pertussis Oxford UK Blackwell Science Ltd 1997 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Bertin, Philippe verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 24(1997), 4, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:24 year:1997 number:4 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 24 1997 4 0 |
| source |
In Molecular microbiology 24(1997), 4, Seite 0 volume:24 year:1997 number:4 pages:0 |
| sourceStr |
In Molecular microbiology 24(1997), 4, Seite 0 volume:24 year:1997 number:4 pages:0 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Molecular microbiology |
| authorswithroles_txt_mv |
Goyard, Sophie @@aut@@ Bertin, Philippe @@aut@@ |
| publishDateDaySort_date |
1997-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ243926537 |
| id |
NLEJ243582749 |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243582749</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707183036.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s1997 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1365-2958.1997.3891753.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243582749</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Goyard, Sophie</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization of BpH3, an H-NS-like protein in Bordetella pertussis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">1997</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2003</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2003||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bertin, Philippe</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Molecular microbiology</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1987</subfield><subfield code="g">24(1997), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926537</subfield><subfield code="w">(DE-600)1501537-3</subfield><subfield code="x">1365-2958</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:24</subfield><subfield code="g">year:1997</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">24</subfield><subfield code="j">1997</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
| author |
Goyard, Sophie |
| spellingShingle |
Goyard, Sophie Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| authorStr |
Goyard, Sophie |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243926537 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut |
| collection |
NL |
| publishPlace |
Oxford UK |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1365-2958 |
| topic_title |
Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| publisher |
Blackwell Science Ltd |
| publisherStr |
Blackwell Science Ltd |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| hierarchy_parent_title |
Molecular microbiology |
| hierarchy_parent_id |
NLEJ243926537 |
| hierarchy_top_title |
Molecular microbiology |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ243926537 (DE-600)1501537-3 |
| title |
Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| ctrlnum |
(DE-627)NLEJ243582749 |
| title_full |
Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| author_sort |
Goyard, Sophie |
| journal |
Molecular microbiology |
| journalStr |
Molecular microbiology |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1997 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Goyard, Sophie Bertin, Philippe |
| container_volume |
24 |
| physical |
Online-Ressource |
| format_se |
Elektronische Aufsätze |
| author-letter |
Goyard, Sophie |
| doi_str_mv |
10.1046/j.1365-2958.1997.3891753.x |
| author2-role |
verfasserin |
| title_sort |
characterization of bph3, an h-ns-like protein in bordetella pertussis |
| title_auth |
Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| abstract |
This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. |
| abstractGer |
This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. |
| abstract_unstemmed |
This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria. |
| collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
| container_issue |
4 |
| title_short |
Characterization of BpH3, an H-NS-like protein in Bordetella pertussis |
| url |
http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x |
| remote_bool |
true |
| author2 |
Bertin, Philippe |
| author2Str |
Bertin, Philippe |
| ppnlink |
NLEJ243926537 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| doi_str |
10.1046/j.1365-2958.1997.3891753.x |
| up_date |
2024-07-06T05:55:48.958Z |
| _version_ |
1803807987028983808 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243582749</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707183036.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s1997 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1365-2958.1997.3891753.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243582749</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Goyard, Sophie</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization of BpH3, an H-NS-like protein in Bordetella pertussis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">1997</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">This study describes the characterization of BpH3, a Bordetella pertussis DNA-binding protein. Sequence analysis reveals significant homology with the H-NS sequence of Escherichia coli and Haemophilus influenzae, particularly in the C-terminal part of the proteins. Our results provide evidence that H-NS and BpH3 display functional homology. First, expression of BpH3 in an hns mutant results in restoration of motility, an H-NS-dependent phenotype. This effect is dependent on the level of BpH3 expression and results from transcriptional activation of the flagellar master operon. Second, the high level of β-glucosidase associated with hns mutations is reversed to the low wild-type level in the presence of BpH3. Third, BpH3 is able, like H-NS, to preferentially bind in vitro to curved DNA fragments, such as flhDC and bla promoter regions. Our results are the first demonstration that proteins homologous to H-NS exist in bacteria phylogenetically distant from H. influenzae and enterobacteria.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2003</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2003||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bertin, Philippe</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Molecular microbiology</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1987</subfield><subfield code="g">24(1997), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926537</subfield><subfield code="w">(DE-600)1501537-3</subfield><subfield code="x">1365-2958</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:24</subfield><subfield code="g">year:1997</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1365-2958.1997.3891753.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">24</subfield><subfield code="j">1997</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.3995314 |