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An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA
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1 reference
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Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
title
An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA
(English)
1 reference
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Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
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9 November 2019
author
Gleb Bourenkov
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2
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Europe PubMed Central
PubMed ID
11430821
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
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9 November 2019
Markus C Wahl
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5
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Europe PubMed Central
PubMed ID
11430821
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
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9 November 2019
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M Worbs
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1
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Europe PubMed Central
PubMed ID
11430821
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9 November 2019
H D Bartunik
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3
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PubMed ID
11430821
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9 November 2019
R Huber
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4
1 reference
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Europe PubMed Central
PubMed ID
11430821
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
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9 November 2019
publication date
1 June 2001
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Europe PubMed Central
PubMed ID
11430821
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
published in
Molecular Cell
1 reference
stated in
Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
volume
7
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Europe PubMed Central
PubMed ID
11430821
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retrieved
9 November 2019
page(s)
1177-1189
1 reference
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Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
issue
6
1 reference
stated in
Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
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9 November 2019
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Escherichia coli-Salmonella typhimurium hybrid nusA genes: identification of a short motif required for action of the lambda N transcription antitermination protein
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Transcription antitermination in vitro by lambda N gene product: requirement for a phage nut site and the products of host nusA, nusB, and nusE genes
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Effects of NusA protein on transcription termination in the tryptophan operon of Escherichia coli
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Evidence that a nucleotide sequence, "boxA," is involved in the action of the NusA protein.
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The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid.
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Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex
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Escherichia coli sigma 70 and NusA proteins. II. Physical properties and self-association states.
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The nusA gene protein of Escherichia coli. Its identification and a demonstration that it interacts with the gene N transcription anti-termination protein of bacteriophage lambda
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An elongation control particle containing the N gene transcriptional antitermination protein of bacteriophage lambda.
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Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein
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The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain
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In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein
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tRNA is entrapped in similar, but distinct, nuclear and cytoplasmic ribonucleoprotein complexes, both of which contain vigilin and elongation factor 1 alpha
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Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains
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Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome
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Antitermination of E. coli rRNA transcription is caused by a control region segment containing lambda nut-like sequences
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Role of Escherichia coli RNA polymerase alpha subunit in modulation of pausing, termination and anti-termination by the transcription elongation factor NusA.
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Functional importance of regions in Escherichia coli elongation factor NusA that interact with RNA polymerase, the bacteriophage lambda N protein and RNA
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The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA
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Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase
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A protein-RNA interaction network facilitates the template-independent cooperative assembly on RNA polymerase of a stable antitermination complex containing the lambda N protein
1 reference
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Information processing by RNA polymerase: recognition of regulatory signals during RNA chain elongation
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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome
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The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome
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7 January 2021
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Conditionally lethal nusAts mutation of Escherichia coli reduces transcription termination but does not affect antitermination of bacteriophage lambda
1 reference
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7 January 2021
based on heuristic
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Recognition of boxA antiterminator RNA by the E. coli antitermination factors NusB and ribosomal protein S10.
1 reference
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Identification and characterization of transcription termination sites in the Escherichia coli lacZ gene.
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lambda N antitermination system: functional analysis of phage interactions with the host NusA protein.
1 reference
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Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
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Amplification and isolation of E. coli nusA protein and studies of its effects on in vitro RNA chain elongation
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Domain organization of the Escherichia coli RNA polymerase sigma 70 subunit
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The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
1 reference
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7 January 2021
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Crystal structure of the GreA transcript cleavage factor from Escherichia coli
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7 January 2021
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Targeted protein footprinting: where different transcription factors bind to RNA polymerase
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nusA amber mutation that causes temperature-sensitive growth of Escherichia coli
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RNA recognition by RNP proteins during RNA processing.
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inferred from DOI database lookup
NusA is required for ribosomal antitermination and for modulation of the transcription elongation rate of both antiterminated RNA and mRNA.
1 reference
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Purification and nucleic-acid-binding properties of a Saccharomyces cerevisiae protein involved in the control of ploidy
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Ribosomal protein L4 and transcription factor NusA have separable roles in mediating terminating of transcription within the leader of the S10 operon of Escherichia coli
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Reduced Rho-dependent transcription termination permits NusA-independent growth of Escherichia coli.
1 reference
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based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S1097-2765(01)00262-3
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683997
stated in
Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
Fatcat ID
release_5hqmmiilbzafjp6jv5lfaemzmm
1 reference
stated in
Fatcat
reference URL
https://api.fatcat.wiki/v0/release/5hqmmiilbzafjp6jv5lfaemzmm
retrieved
24 November 2022
based on heuristic
mapped directly with Wikidata item
OpenCitations bibliographic resource ID
1683997
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683997
PubMed ID
11430821
2 references
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1683997
stated in
Europe PubMed Central
PubMed ID
11430821
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11430821%20AND%20SRC:MED&resulttype=core&format=json
retrieved
9 November 2019
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