The phage λ gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase
Identifieur interne : 004745 ( Main/Exploration ); précédent : 004744; suivant : 004746The phage λ gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase
Auteurs : William S. Yarnell [États-Unis] ; Jeffrey W. Roberts [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1992.
English descriptors
- Teeft :
- Antiterminating form, Antitermination, Antiterminator, Biol, Bottom strand, Control experiments, Cornell university, Digestion, Digestion time, Dna, Early elongation pause, Early pause, Elongation, Elongation properties, Experimental procedures, Footprint, Footprinting, Grayhack, Initiation complexes, Initiation factor, Kinetic barrier, Late gene promoter, Late gene promoter segments, Little effect, Mutant, Mutant complexes, Mutant dnas, Mutation, Natural pause, Natural pause site, Nonpausing, Nonpausing mutations, Ntps, Nucleotide, Nucleotide deprivation, Nusa, Nusa protein, Open promoter, Open promoter complexes, Pause site, Pause sites, Phage, Polymerase, Promoter, Promoter elements, Promoter region, Reaction mixtures, Rnap, Sequencing, Strong protection, Terminator, Terminator readthrough, Transcription, Transcription antitermination, Transcription antiterminator, Transcription bubble, Transcription buffer, Transcription complexes, Transcription factor nusa, Unpublished data, Wild type.
Abstract
Abstract: The bacteriophage λ gene Q transcription antiterminator modifies RNA polymerase during an extended pause in elongation at nt +16 and +17 of the phage late gene promoter transcript. We show here that Q binds a specific DNA site between the −10 and −35 elements of the promoter as it interacts with the enzyme. We show that the pause must reflect a specialized elongation structure that is receptive to modification by Q, because Q does not bind to RNA polymerase stopped artificially after transcribing 16 nt of mutant DNA that does not encode the natural pause. Footprinting shows that RNA polymerase in the paused complex makes distinctive interactions with DNA in the region where Q binds; binding of Q, in turn, changes the footprint both at the Q-binding site and in the transcription bubble. Binding of Q to the paused transcription complex is stabilized by the transcription factor NusA, as expected from the dependence of λ Q-mediated anti-termination on NusA.
Url:
DOI: 10.1016/0092-8674(92)90639-T
Affiliations:
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Yarnell</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Section of Biochemistry, Molecular and Cell Biology Biotechnology Building Cornell University Ithaca</wicri:cityArea></affiliation></author><author><name sortKey="Roberts, Jeffrey W" sort="Roberts, Jeffrey W" uniqKey="Roberts J" first="Jeffrey W." last="Roberts">Jeffrey W. Roberts</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Section of Biochemistry, Molecular and Cell Biology Biotechnology Building Cornell University Ithaca</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">69</biblScope><biblScope unit="issue">7</biblScope><biblScope unit="page" from="1181">1181</biblScope><biblScope unit="page" to="1189">1189</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Antiterminating form</term><term>Antitermination</term><term>Antiterminator</term><term>Biol</term><term>Bottom strand</term><term>Control experiments</term><term>Cornell university</term><term>Digestion</term><term>Digestion time</term><term>Dna</term><term>Early elongation pause</term><term>Early pause</term><term>Elongation</term><term>Elongation properties</term><term>Experimental procedures</term><term>Footprint</term><term>Footprinting</term><term>Grayhack</term><term>Initiation complexes</term><term>Initiation factor</term><term>Kinetic barrier</term><term>Late gene promoter</term><term>Late gene promoter segments</term><term>Little effect</term><term>Mutant</term><term>Mutant complexes</term><term>Mutant dnas</term><term>Mutation</term><term>Natural pause</term><term>Natural pause site</term><term>Nonpausing</term><term>Nonpausing mutations</term><term>Ntps</term><term>Nucleotide</term><term>Nucleotide deprivation</term><term>Nusa</term><term>Nusa protein</term><term>Open promoter</term><term>Open promoter complexes</term><term>Pause site</term><term>Pause sites</term><term>Phage</term><term>Polymerase</term><term>Promoter</term><term>Promoter elements</term><term>Promoter region</term><term>Reaction mixtures</term><term>Rnap</term><term>Sequencing</term><term>Strong protection</term><term>Terminator</term><term>Terminator readthrough</term><term>Transcription</term><term>Transcription antitermination</term><term>Transcription antiterminator</term><term>Transcription bubble</term><term>Transcription buffer</term><term>Transcription complexes</term><term>Transcription factor nusa</term><term>Unpublished data</term><term>Wild type</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The bacteriophage λ gene Q transcription antiterminator modifies RNA polymerase during an extended pause in elongation at nt +16 and +17 of the phage late gene promoter transcript. We show here that Q binds a specific DNA site between the −10 and −35 elements of the promoter as it interacts with the enzyme. We show that the pause must reflect a specialized elongation structure that is receptive to modification by Q, because Q does not bind to RNA polymerase stopped artificially after transcribing 16 nt of mutant DNA that does not encode the natural pause. Footprinting shows that RNA polymerase in the paused complex makes distinctive interactions with DNA in the region where Q binds; binding of Q, in turn, changes the footprint both at the Q-binding site and in the transcription bubble. Binding of Q to the paused transcription complex is stabilized by the transcription factor NusA, as expected from the dependence of λ Q-mediated anti-termination on NusA.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Yarnell, William S" sort="Yarnell, William S" uniqKey="Yarnell W" first="William S." last="Yarnell">William S. Yarnell</name></region><name sortKey="Roberts, Jeffrey W" sort="Roberts, Jeffrey W" uniqKey="Roberts J" first="Jeffrey W." last="Roberts">Jeffrey W. Roberts</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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