Eintrag weiter verarbeiten
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities
Gespeichert in:
| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Journal of Bacteriology, 192, 2010, 11, S. 2670-2681 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua |
|---|---|
| author |
Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua |
| spellingShingle |
Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua Journal of Bacteriology Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities Molecular Biology Microbiology |
| author_sort |
li, jie |
| spelling |
Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.01511-09 <jats:title>ABSTRACT</jats:title> <jats:p> Primase, encoded by <jats:italic>dnaG</jats:italic> in bacteria, is a specialized DNA-dependent RNA polymerase that synthesizes RNA primers <jats:italic>de novo</jats:italic> for elongation by DNA polymerase. Genome sequence analysis has revealed two distantly related <jats:italic>dnaG</jats:italic> genes, <jats:italic>TtdnaG</jats:italic> and <jats:italic>TtdnaG</jats:italic> <jats:sub>2</jats:sub> , in the thermophilic bacterium <jats:italic>Thermoanaerobacter tengcongensis</jats:italic> . Both TtDnaG (600 amino acids) and TtDnaG2 (358 amino acids) exhibit primase activities <jats:italic>in vitro</jats:italic> at a wide range of temperatures. Interestingly, the template recognition specificities of these two primases are quite distinctive. When trinucleotide-specific templates were tested, TtDnaG initiated RNA primer synthesis efficiently only on templates containing the trinucleotide 5′-CCC-3′, not on the other 63 possible trinucleotides. When the 5′-CCC-3′ sequence was flanked by additional cytosines or guanines, the initiation efficiency of TtDnaG increased remarkably. Significantly, TtDnaG could specifically and efficiently initiate RNA primer synthesis on a limited set of tetranucleotides composed entirely of cytosines and guanines, indicating that TtDnaG initiated RNA primer synthesis more preferably on GC-containing tetranucleotides. In contrast, it seemed that TtDnaG2 had no specific initiation nucleotides, as it could efficiently initiate RNA primer synthesis on all templates tested. The DNA binding affinity of TtDnaG2 was usually 10-fold higher than that of TtDnaG, which might correlate with its high activity but low template specificity. These distinct priming activities and specificities of TtDnaG and TtDnaG2 might shed new light on the diversity in the structure and function of the primases. </jats:p> Two Distantly Homologous DnaG Primases from <i>Thermoanaerobacter tengcongensis</i> Exhibit Distinct Initiation Specificities and Priming Activities Journal of Bacteriology |
| doi_str_mv |
10.1128/jb.01511-09 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMTUxMS0wOQ |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMTUxMS0wOQ |
| institution |
DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 |
| imprint |
American Society for Microbiology, 2010 |
| imprint_str_mv |
American Society for Microbiology, 2010 |
| issn |
1098-5530 0021-9193 |
| issn_str_mv |
1098-5530 0021-9193 |
| language |
English |
| mega_collection |
American Society for Microbiology (CrossRef) |
| match_str |
li2010twodistantlyhomologousdnagprimasesfromthermoanaerobactertengcongensisexhibitdistinctinitiationspecificitiesandprimingactivities |
| publishDateSort |
2010 |
| publisher |
American Society for Microbiology |
| recordtype |
ai |
| record_format |
ai |
| series |
Journal of Bacteriology |
| source_id |
49 |
| title |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_unstemmed |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_full |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_fullStr |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_full_unstemmed |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_short |
Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_sort |
two distantly homologous dnag primases from
<i>thermoanaerobacter tengcongensis</i>
exhibit distinct initiation specificities and priming activities |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.01511-09 |
| publishDate |
2010 |
| physical |
2670-2681 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
Primase, encoded by
<jats:italic>dnaG</jats:italic>
in bacteria, is a specialized DNA-dependent RNA polymerase that synthesizes RNA primers
<jats:italic>de novo</jats:italic>
for elongation by DNA polymerase. Genome sequence analysis has revealed two distantly related
<jats:italic>dnaG</jats:italic>
genes,
<jats:italic>TtdnaG</jats:italic>
and
<jats:italic>TtdnaG</jats:italic>
<jats:sub>2</jats:sub>
, in the thermophilic bacterium
<jats:italic>Thermoanaerobacter tengcongensis</jats:italic>
. Both TtDnaG (600 amino acids) and TtDnaG2 (358 amino acids) exhibit primase activities
<jats:italic>in vitro</jats:italic>
at a wide range of temperatures. Interestingly, the template recognition specificities of these two primases are quite distinctive. When trinucleotide-specific templates were tested, TtDnaG initiated RNA primer synthesis efficiently only on templates containing the trinucleotide 5′-CCC-3′, not on the other 63 possible trinucleotides. When the 5′-CCC-3′ sequence was flanked by additional cytosines or guanines, the initiation efficiency of TtDnaG increased remarkably. Significantly, TtDnaG could specifically and efficiently initiate RNA primer synthesis on a limited set of tetranucleotides composed entirely of cytosines and guanines, indicating that TtDnaG initiated RNA primer synthesis more preferably on GC-containing tetranucleotides. In contrast, it seemed that TtDnaG2 had no specific initiation nucleotides, as it could efficiently initiate RNA primer synthesis on all templates tested. The DNA binding affinity of TtDnaG2 was usually 10-fold higher than that of TtDnaG, which might correlate with its high activity but low template specificity. These distinct priming activities and specificities of TtDnaG and TtDnaG2 might shed new light on the diversity in the structure and function of the primases.
</jats:p> |
| container_issue |
11 |
| container_start_page |
2670 |
| container_title |
Journal of Bacteriology |
| container_volume |
192 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792329123992961024 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T13:04:09.76Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Two+Distantly+Homologous+DnaG+Primases+from++++++++++++Thermoanaerobacter+tengcongensis++++++++++++Exhibit+Distinct+Initiation+Specificities+and+Priming+Activities&rft.date=2010-06-01&genre=article&issn=1098-5530&volume=192&issue=11&spage=2670&epage=2681&pages=2670-2681&jtitle=Journal+of+Bacteriology&atitle=Two+Distantly+Homologous+DnaG+Primases+from%0A++++++++++++%3Ci%3EThermoanaerobacter+tengcongensis%3C%2Fi%3E%0A++++++++++++Exhibit+Distinct+Initiation+Specificities+and+Priming+Activities&aulast=Xiang&aufirst=Hua&rft_id=info%3Adoi%2F10.1128%2Fjb.01511-09&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792329123992961024 |
| author | Li, Jie, Liu, Jingfang, Zhou, Ligang, Pei, Huadong, Zhou, Jian, Xiang, Hua |
| author_facet | Li, Jie, Liu, Jingfang, Zhou, Ligang, Pei, Huadong, Zhou, Jian, Xiang, Hua, Li, Jie, Liu, Jingfang, Zhou, Ligang, Pei, Huadong, Zhou, Jian, Xiang, Hua |
| author_sort | li, jie |
| container_issue | 11 |
| container_start_page | 2670 |
| container_title | Journal of Bacteriology |
| container_volume | 192 |
| description | <jats:title>ABSTRACT</jats:title> <jats:p> Primase, encoded by <jats:italic>dnaG</jats:italic> in bacteria, is a specialized DNA-dependent RNA polymerase that synthesizes RNA primers <jats:italic>de novo</jats:italic> for elongation by DNA polymerase. Genome sequence analysis has revealed two distantly related <jats:italic>dnaG</jats:italic> genes, <jats:italic>TtdnaG</jats:italic> and <jats:italic>TtdnaG</jats:italic> <jats:sub>2</jats:sub> , in the thermophilic bacterium <jats:italic>Thermoanaerobacter tengcongensis</jats:italic> . Both TtDnaG (600 amino acids) and TtDnaG2 (358 amino acids) exhibit primase activities <jats:italic>in vitro</jats:italic> at a wide range of temperatures. Interestingly, the template recognition specificities of these two primases are quite distinctive. When trinucleotide-specific templates were tested, TtDnaG initiated RNA primer synthesis efficiently only on templates containing the trinucleotide 5′-CCC-3′, not on the other 63 possible trinucleotides. When the 5′-CCC-3′ sequence was flanked by additional cytosines or guanines, the initiation efficiency of TtDnaG increased remarkably. Significantly, TtDnaG could specifically and efficiently initiate RNA primer synthesis on a limited set of tetranucleotides composed entirely of cytosines and guanines, indicating that TtDnaG initiated RNA primer synthesis more preferably on GC-containing tetranucleotides. In contrast, it seemed that TtDnaG2 had no specific initiation nucleotides, as it could efficiently initiate RNA primer synthesis on all templates tested. The DNA binding affinity of TtDnaG2 was usually 10-fold higher than that of TtDnaG, which might correlate with its high activity but low template specificity. These distinct priming activities and specificities of TtDnaG and TtDnaG2 might shed new light on the diversity in the structure and function of the primases. </jats:p> |
| doi_str_mv | 10.1128/jb.01511-09 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4wMTUxMS0wOQ |
| imprint | American Society for Microbiology, 2010 |
| imprint_str_mv | American Society for Microbiology, 2010 |
| institution | DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15 |
| issn | 1098-5530, 0021-9193 |
| issn_str_mv | 1098-5530, 0021-9193 |
| language | English |
| last_indexed | 2024-03-01T13:04:09.76Z |
| match_str | li2010twodistantlyhomologousdnagprimasesfromthermoanaerobactertengcongensisexhibitdistinctinitiationspecificitiesandprimingactivities |
| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 2670-2681 |
| publishDate | 2010 |
| publishDateSort | 2010 |
| publisher | American Society for Microbiology |
| record_format | ai |
| recordtype | ai |
| series | Journal of Bacteriology |
| source_id | 49 |
| spelling | Li, Jie Liu, Jingfang Zhou, Ligang Pei, Huadong Zhou, Jian Xiang, Hua 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.01511-09 <jats:title>ABSTRACT</jats:title> <jats:p> Primase, encoded by <jats:italic>dnaG</jats:italic> in bacteria, is a specialized DNA-dependent RNA polymerase that synthesizes RNA primers <jats:italic>de novo</jats:italic> for elongation by DNA polymerase. Genome sequence analysis has revealed two distantly related <jats:italic>dnaG</jats:italic> genes, <jats:italic>TtdnaG</jats:italic> and <jats:italic>TtdnaG</jats:italic> <jats:sub>2</jats:sub> , in the thermophilic bacterium <jats:italic>Thermoanaerobacter tengcongensis</jats:italic> . Both TtDnaG (600 amino acids) and TtDnaG2 (358 amino acids) exhibit primase activities <jats:italic>in vitro</jats:italic> at a wide range of temperatures. Interestingly, the template recognition specificities of these two primases are quite distinctive. When trinucleotide-specific templates were tested, TtDnaG initiated RNA primer synthesis efficiently only on templates containing the trinucleotide 5′-CCC-3′, not on the other 63 possible trinucleotides. When the 5′-CCC-3′ sequence was flanked by additional cytosines or guanines, the initiation efficiency of TtDnaG increased remarkably. Significantly, TtDnaG could specifically and efficiently initiate RNA primer synthesis on a limited set of tetranucleotides composed entirely of cytosines and guanines, indicating that TtDnaG initiated RNA primer synthesis more preferably on GC-containing tetranucleotides. In contrast, it seemed that TtDnaG2 had no specific initiation nucleotides, as it could efficiently initiate RNA primer synthesis on all templates tested. The DNA binding affinity of TtDnaG2 was usually 10-fold higher than that of TtDnaG, which might correlate with its high activity but low template specificity. These distinct priming activities and specificities of TtDnaG and TtDnaG2 might shed new light on the diversity in the structure and function of the primases. </jats:p> Two Distantly Homologous DnaG Primases from <i>Thermoanaerobacter tengcongensis</i> Exhibit Distinct Initiation Specificities and Priming Activities Journal of Bacteriology |
| spellingShingle | Li, Jie, Liu, Jingfang, Zhou, Ligang, Pei, Huadong, Zhou, Jian, Xiang, Hua, Journal of Bacteriology, Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities, Molecular Biology, Microbiology |
| title | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_full | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_fullStr | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_full_unstemmed | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_short | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| title_sort | two distantly homologous dnag primases from <i>thermoanaerobacter tengcongensis</i> exhibit distinct initiation specificities and priming activities |
| title_unstemmed | Two Distantly Homologous DnaG Primases from Thermoanaerobacter tengcongensis Exhibit Distinct Initiation Specificities and Priming Activities |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.01511-09 |