Evidence map›Paper›PMID 18537269›Full record

ArticleBiochemistry2008

Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein.

Gretchen Meinke, Chukwudi Ezeokonkwo, Paul Balbo, Walter Stafford, Claire Moore, Andrew Bohm

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 36 citations in OpenAlex.

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  12. Molecular basis for the recognition of the human AAUAAA polyadenylation signal.Proceedings of the National Academy of Sciences of the United States of America · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Gretchen MeinkeDepartment of Biochemistry, Tufts University, 136 Harrison Avenue, Boston, Massachusetts 02111, USA.
Chukwudi Ezeokonkwo
Paul Balbo
Walter Stafford
Claire Moore
Andrew Bohm
Boston Biomedical Research Institute · USTufts University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Molecular mechanism of mRNA 3'-end formation in yeastR01GM041752 · NIGMS · TUFTS UNIVERSITY BOSTON · PI MOORE, CLAIRE L · 1989 to 2010
$4.0M
Mechanism of poly(A) polymerase processivityR01GM065972 · NIGMS · TUFTS UNIVERSITY BOSTON · PI BOHM, ALEX ANDREW · 2002 to 2006
$1.5M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM041752NIGMS NIH HHS GM065972NIGMS NIH HHS R01 GM041752NIGMS NIH HHS R01 GM065972
6 · The paper itself

Abstract

In yeast, the mRNA processing enzyme poly(A) polymerase is tethered to the much larger 3'-end processing complex via Fip1, a 36 kDa protein of unknown structure. We report the 2.6 A crystal structure of yeast poly(A) polymerase in complex with a peptide containing residues 80-105 of Fip1. The Fip1 peptide binds to the outside surface of the C-terminal domain of the polymerase. On the basis of this structure, we designed a mutant of the polymerase (V498Y, C485R) that is lethal to yeast. The mutant is unable to bind Fip1 but retains full polymerase activity. Fip1 is found in all eukaryotes and serves to connect poly(A) polymerase to pre-mRNA processing complexes in yeast, plants, and mammals. However, the Fip1 sequence is highly divergent, and residues on both Pap1 and Fip1 at the observed interaction surface are poorly conserved. Herein we demonstrate using analytical ultracentrifugation, circular dichroism, proteolytic studies, and other techniques that, in the absence of Pap1, Fip1 is largely, if not completely, unfolded. We speculate that flexibility may be important for Fip1's function as a molecular scaffold.

Indexed as

Amino Acid SequenceBiophysical PhenomenaBiophysicsConserved SequenceCrystallography, X-RayHumansKineticsModels, MolecularMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsMutationPancreatitis-Associated ProteinsPeptidesPolynucleotide AdenylyltransferaseProtein BindingProtein Structure, QuaternaryFIP1 protein, S cerevisiaemRNA Cleavage and Polyadenylation FactorsPancreatitis-Associated ProteinsPeptidesPolynucleotide AdenylyltransferaseREG3A protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID18537269
PMCPMC2615413
OpenAlexW1978501040

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.