Purification and characterization of a putative sigma factor from Chalamydomonas reinhardi
Two proteins with sigma-like activity have been isolated from the alga, Chlamydomonas reinhardi. One protein, sigma 2, has been partially purified and appears to have a molecular weight of 51,000. The interaction of this protein with a heterologous (Escherichia coli) and homologous (Chlamydomonas, c...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1976-11, Vol.73 (11), p.3961-3965 |
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| container_issue | 11 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Surzycki, S J Shellenbarger, D L |
| description | Two proteins with sigma-like activity have been isolated from the alga, Chlamydomonas reinhardi. One protein, sigma 2, has been partially purified and appears to have a molecular weight of 51,000. The interaction of this protein with a heterologous (Escherichia coli) and homologous (Chlamydomonas, chloroplast rifampicin-sensitive) core RNA-polymerase (RNA nucleotidyltransferase, nucleosidetriphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) was studied. Sigma 2 protein appears to stimulate the formation of open (rapid starting) binary complexes by both of the core enzymes. Stimulation of transcription by sigma 2 on chloroplast DNA was greater when Chlamydomonas core enzyme was used. Moreover, in vitro transcription on a variety of templates using RNA polymerases I and II from Chlamydomonas was not stimulated by this protein. |
| doi_str_mv | 10.1073/pnas.73.11.3961 |
| format | Article |
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Moreover, in vitro transcription on a variety of templates using RNA polymerases I and II from Chlamydomonas was not stimulated by this protein.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.73.11.3961</identifier><identifier>PMID: 792879</identifier><language>eng</language><publisher>United States: National Acad Sciences</publisher><subject>Chlamydomonas - analysis ; Chlamydomonas - enzymology ; Chloroplasts - metabolism ; DNA-Directed RNA Polymerases - antagonists & inhibitors ; DNA-Directed RNA Polymerases - metabolism ; Escherichia coli - enzymology ; Molecular Weight ; Rifampin - pharmacology ; Sigma Factor - isolation & purification ; Sigma Factor - metabolism ; Templates, Genetic ; Transcription Factors - isolation & purification ; Transcription, Genetic</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1976-11, Vol.73 (11), p.3961-3965</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3541-13c24ba683725f81247016d39c09458bc46d51abd5b7e4f3937e89d9563737d13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/73/11.cover.gif</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC431283/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC431283/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/792879$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Surzycki, S J</creatorcontrib><creatorcontrib>Shellenbarger, D L</creatorcontrib><title>Purification and characterization of a putative sigma factor from Chalamydomonas reinhardi</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Two proteins with sigma-like activity have been isolated from the alga, Chlamydomonas reinhardi. One protein, sigma 2, has been partially purified and appears to have a molecular weight of 51,000. The interaction of this protein with a heterologous (Escherichia coli) and homologous (Chlamydomonas, chloroplast rifampicin-sensitive) core RNA-polymerase (RNA nucleotidyltransferase, nucleosidetriphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) was studied. Sigma 2 protein appears to stimulate the formation of open (rapid starting) binary complexes by both of the core enzymes. Stimulation of transcription by sigma 2 on chloroplast DNA was greater when Chlamydomonas core enzyme was used. Moreover, in vitro transcription on a variety of templates using RNA polymerases I and II from Chlamydomonas was not stimulated by this protein.</description><subject>Chlamydomonas - analysis</subject><subject>Chlamydomonas - enzymology</subject><subject>Chloroplasts - metabolism</subject><subject>DNA-Directed RNA Polymerases - antagonists & inhibitors</subject><subject>DNA-Directed RNA Polymerases - metabolism</subject><subject>Escherichia coli - enzymology</subject><subject>Molecular Weight</subject><subject>Rifampin - pharmacology</subject><subject>Sigma Factor - isolation & purification</subject><subject>Sigma Factor - metabolism</subject><subject>Templates, Genetic</subject><subject>Transcription Factors - isolation & purification</subject><subject>Transcription, Genetic</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kb1PHDEQxS2UQC5ATYMiV6Taw7P2ru0iRXQiHxISFKRJY3n9wRntri_2Lgr89fHpTqekSTWaeb83HvkhdAFkCYTT682o85LTJcCSyhaO0AKIhKplkrxBC0JqXglWs3fofc5PhBDZCHKCjrmsBZcL9PN-TsEHo6cQR6xHi81aJ20ml8Lrbhg91ngzT6V7djiHx0FjX4iYsE9xwKu17vXwYuMQyy04uTCWFTacobde99md7-sp-vHl5mH1rbq9-_p99fm2MrRhUAE1Net0KyivGy-gZpxAa6k0RLJGdIa1tgHd2abjjnkqKXdCWtm0lFNugZ6iT7u9m7kbnDVunJLu1SaFQacXFXVQ_ypjWKvH-KwYhVrQ4r_a-1P8Nbs8qSFk4_pejy7OWQnaUtEIUcDrHWhSzDk5f3gDiNqGobZhqFIB1DaM4rj8-7QDv_v9In_cy1vfQTz4lZ_7fnK_p0J--C9J_wBq659E</recordid><startdate>19761101</startdate><enddate>19761101</enddate><creator>Surzycki, S J</creator><creator>Shellenbarger, D L</creator><general>National Acad Sciences</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19761101</creationdate><title>Purification and characterization of a putative sigma factor from Chalamydomonas reinhardi</title><author>Surzycki, S J ; Shellenbarger, D L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3541-13c24ba683725f81247016d39c09458bc46d51abd5b7e4f3937e89d9563737d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Chlamydomonas - analysis</topic><topic>Chlamydomonas - enzymology</topic><topic>Chloroplasts - metabolism</topic><topic>DNA-Directed RNA Polymerases - antagonists & inhibitors</topic><topic>DNA-Directed RNA Polymerases - metabolism</topic><topic>Escherichia coli - enzymology</topic><topic>Molecular Weight</topic><topic>Rifampin - pharmacology</topic><topic>Sigma Factor - isolation & purification</topic><topic>Sigma Factor - metabolism</topic><topic>Templates, Genetic</topic><topic>Transcription Factors - isolation & purification</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Surzycki, S J</creatorcontrib><creatorcontrib>Shellenbarger, D L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Surzycki, S J</au><au>Shellenbarger, D L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a putative sigma factor from Chalamydomonas reinhardi</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1976-11-01</date><risdate>1976</risdate><volume>73</volume><issue>11</issue><spage>3961</spage><epage>3965</epage><pages>3961-3965</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Two proteins with sigma-like activity have been isolated from the alga, Chlamydomonas reinhardi. One protein, sigma 2, has been partially purified and appears to have a molecular weight of 51,000. The interaction of this protein with a heterologous (Escherichia coli) and homologous (Chlamydomonas, chloroplast rifampicin-sensitive) core RNA-polymerase (RNA nucleotidyltransferase, nucleosidetriphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) was studied. Sigma 2 protein appears to stimulate the formation of open (rapid starting) binary complexes by both of the core enzymes. Stimulation of transcription by sigma 2 on chloroplast DNA was greater when Chlamydomonas core enzyme was used. Moreover, in vitro transcription on a variety of templates using RNA polymerases I and II from Chlamydomonas was not stimulated by this protein.</abstract><cop>United States</cop><pub>National Acad Sciences</pub><pmid>792879</pmid><doi>10.1073/pnas.73.11.3961</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1976-11, Vol.73 (11), p.3961-3965 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Chlamydomonas - analysis Chlamydomonas - enzymology Chloroplasts - metabolism DNA-Directed RNA Polymerases - antagonists & inhibitors DNA-Directed RNA Polymerases - metabolism Escherichia coli - enzymology Molecular Weight Rifampin - pharmacology Sigma Factor - isolation & purification Sigma Factor - metabolism Templates, Genetic Transcription Factors - isolation & purification Transcription, Genetic |
| title | Purification and characterization of a putative sigma factor from Chalamydomonas reinhardi |
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