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Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae
scientific article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
22575652
retrieved
1 December 2016
title
Novel interactions at the essential N-terminus of poly(A) polymerase that could regulate poly(A) addition in Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
22575652
retrieved
1 December 2016
main subject
biophysics
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cell biology
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structural biology
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Saccharomyces cerevisiae
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Cleavage polyadenylation factor subunit FIP1 YJR093C
1 reference
stated in
GOA release 2020-03-11
RNA-processing protein PTA1 YAL043C
1 reference
stated in
GOA release 2020-03-11
Polynucleotide adenylyltransferase PAP1 YKR002W
1 reference
stated in
GOA release 2020-03-11
Nab6p YML117W
1 reference
stated in
GOA release 2020-03-11
Cleavage/polyadenylation factor CFT1 YDR301W
1 reference
stated in
GOA release 2020-03-11
author name string
Chukwudi Ezeokonkwo
series ordinal
1
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Mohamed A Ghazy
series ordinal
2
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Alexander Zhelkovsky
series ordinal
3
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Pei-Chun Yeh
series ordinal
4
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Claire Moore
series ordinal
5
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language of work or name
English
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publication date
24 April 2012
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published in
FEBS Letters
1 reference
stated in
PubMed
PubMed ID
22575652
retrieved
1 December 2016
volume
586
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issue
8
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page(s)
1173-8
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cites work
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Nuclear mRNA surveillance in THO/sub2 mutants is triggered by inefficient polyadenylation
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Structure of Yeast Poly(A) Polymerase in Complex with a Peptide from Fip1, an Intrinsically Disordered Protein † ‡
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Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase
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Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination
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Fip1 regulates the activity of Poly(A) polymerase through multiple interactions
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The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation
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To polyadenylate or to deadenylate: that is the question
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The essential N terminus of the Pta1 scaffold protein is required for snoRNA transcription termination and Ssu72 function but is dispensable for pre-mRNA 3'-end processing.
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Rrp6, rrp47 and cofactors of the nuclear exosome
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Crossref
reference URL
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Identification of new poly(A) polymerase-inhibitory proteins capable of regulating pre-mRNA polyadenylation
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22575652
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Structure-function relationships in the Saccharomyces cerevisiae poly(A) polymerase. Identification of a novel RNA binding site and a domain that interacts with specificity factor(s)
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22575652
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.FEBSLET.2012.03.036
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2568223
OpenCitations bibliographic resource ID
2568223
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2568223
PMCID
3587332
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2568223
PubMed ID
22575652
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2568223
ResearchGate publication ID
224938960
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