Evidence map›Paper›PMID 19690099›Full record

ArticleRNA (New York, N.Y.)2009

Structure-activity relationships in human RNA 3'-phosphate cyclase.

Naoko Tanaka, Stewart Shuman

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structures of RNA 3'-phosphate cyclase bound to ATP reveal the mechanism of nucleotidyl transfer and metal-assisted catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  7. Article
  8. Article
  9. Article
  10. Archaeal 3'-phosphate RNA splicing ligase characterization identifies the missing component in tRNA maturation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. 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

2 authors at 1 institution in 1 country.

Naoko TanakaSloan-Kettering Institute, New York, New York 10065, USA.
Stewart Shuman
Kettering University · US

Funding

Vaccina Virus DNA TopoisomeraseR37GM046330 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI SHUMAN, STEWART H · 2007 to 2016
$6.1M
VACCINIA VIRUS DNA TOPOISOMERASE IR01GM046330 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 1991 to 2006
$3.1M
NIGMS NIH HHS GM46330NIGMS NIH HHS R01 GM046330NIGMS NIH HHS R37 GM046330
6 · The paper itself

Abstract

RNA 3'-phosphate cyclase (Rtc) enzymes are a widely distributed family that catalyze the synthesis of RNA 2',3' cyclic phosphate ends via an ATP-dependent pathway comprising three nucleotidyl transfer steps: reaction of Rtc with ATP to form a covalent Rtc-(histidinyl-N)-AMP intermediate and release PP(i); transfer of AMP from Rtc1 to an RNA 3'-phosphate to form an RNA(3')pp(5')A intermediate; and attack by the terminal nucleoside O2' on the 3'-phosphate to form an RNA 2',3' cyclic phosphate product and release AMP. Here we used the crystal structure of Escherichia coli RtcA to guide a mutational analysis of the human RNA cyclase Rtc1. An alanine scan defined seven conserved residues as essential for the Rtc1 RNA cyclization and autoadenylylation reactions. Structure-activity relationships were clarified by conservative substitutions. Our results are consistent with a mechanism of adenylate transfer in which attack of the Rtc1 His320 nucleophile on the ATP alpha phosphorus is facilitated by proper orientation of the PP(i) leaving group via contacts to Arg21, Arg40, and Arg43. We invoke roles for Tyr294 in binding the adenine base and Glu14 in binding the divalent cation cofactor. We find that Rtc1 forms a stable binary complex with a 3'-phosphate terminated RNA, but not with an otherwise identical 3'-OH terminated RNA. Mutation of His320 had little impact on RNA 3'-phosphate binding, signifying that covalent adenylylation of Rtc1 is not a prerequisite for end recognition.

Indexed as

Amino Acid SequenceBiocatalysisCatalytic DomainEscherichia coliHumansLigasesMolecular Sequence DataMutagenesisRecombinant ProteinsSequence Homology, Amino AcidStructure-Activity RelationshipLigasesRecombinant ProteinsRNA 3'-terminal phosphate cyclase

Identifiers

PMID19690099
PMCPMC2743044
OpenAlexW2107773276

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.