Evidence map›Paper›PMID 16275784›Full record

ArticleNucleic acids research2005

Structure-function analysis of yeast RNA debranching enzyme (Dbr1), a manganese-dependent phosphodiesterase.

M Fahad Khalid, Masad J Damha, Stewart Shuman, Beate Schwer

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

41 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. All-atom simulations disentangle the functional dynamics underlying gene maturation in the intron lariat spliceosome.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Unexplored Molecular Features of theFrontiers in cellular and infection microbiology · 2018
    Article
  17. Article
  18. Article
  19. Metal dependence and branched RNA cocrystal structures of the RNA lariat debranching enzyme Dbr1.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  20. Article
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

4 authors at 1 institution in 1 country.

M Fahad KhalidDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.
Masad J Damha
Stewart Shuman
Beate Schwer
Cornell University · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF SPLICEOSOMAL ATPASESR01GM050288 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHWER, BEATE · 1994 to 2011
$3.9M
NIGMS NIH HHS GM50288NIGMS NIH HHS R01 GM050288
6 · The paper itself

Abstract

Saccharomyces cerevisiae Dbr1 is a 405-amino acid RNA debranching enzyme that cleaves the 2'-5' phosphodiester bonds of the lariat introns formed during pre-mRNA splicing. Debranching appears to be a rate-limiting step for the turnover of intronic RNA, insofar as the steady-state levels of lariat introns are greatly increased in a Deltadbr1 strain. To gain insight to the requirements for yeast Dbr1 function, we performed a mutational analysis of 28 amino acids that are conserved in Dbr1 homologs from other organisms. We identified 13 residues (His13, Asp40, Arg45, Asp49, Tyr68, Tyr69, Asn85, His86, Glu87, His179, Asp180, His231 and His233) at which alanine substitutions resulted in lariat intron accumulation in vivo. Conservative replacements at these positions were introduced to illuminate structure-activity relationships. Residues important for Dbr1 function include putative counterparts of the amino acids that comprise the active site of the metallophosphoesterase superfamily, exemplified by the DNA phosphodiesterase Mre11. Using natural lariat RNAs and synthetic branched RNAs as substrates, we found that mutation of Asp40, Asn85, His86, His179, His231 or His233 to alanine abolishes or greatly diminishes debranching activity in vitro. Dbr1 sediments as a monomer and requires manganese as the metal cofactor for debranching.

Indexed as

AlanineAmino Acid SequenceDNA Mutational AnalysisIntronsManganeseMolecular Sequence DataPhosphoric Diester HydrolasesRNA NucleotidyltransferasesSaccharomyces cerevisiae ProteinsSequence AlignmentStructure-Activity RelationshipAlanineManganesemRNA debranching enzymePhosphoric Diester HydrolasesRNA debranching enzyme Dbr1, S cerevisiaeRNA NucleotidyltransferasesSaccharomyces cerevisiae Proteins

Identifiers

PMID16275784
PMCPMC1278944
OpenAlexW2115449902

What OpenQuestion holds

Textmetadata
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.