Evidence map›Paper›PMID 16428247›Full record

ArticleNucleic acids research2006

Structure-function analysis of the kinase-CPD domain of yeast tRNA ligase (Trl1) and requirements for complementation of tRNA splicing by a plant Trl1 homolog.

Li Kai Wang, Beate Schwer, Markus Englert, Hildburg Beier, Stewart Shuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

42 citing papers in PubMed, 58 citations in OpenAlex.

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  4. Fungi of the order Mucorales express a "sealing-only" tRNA ligase.bioRxiv : the preprint server for biology · 2023
    Article
  5. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
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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

5 authors at 1 institution in 1 country.

Li Kai WangMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
Beate Schwer
Markus Englert
Hildburg Beier
Stewart Shuman
Kettering University · US

Funding

Viral RNA Modifying EnzymesR01GM042498 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 1989 to 2017
$6.8M
NIGMS NIH HHS GM42498NIGMS NIH HHS R01 GM042498
6 · The paper itself

Abstract

Trl1 is an essential 827 amino acid enzyme that executes the end-healing and end-sealing steps of tRNA splicing in Saccharomyces cerevisiae. Trl1 consists of two domains--an N-terminal ligase component and a C-terminal 5'-kinase/2',3'-cyclic phosphodiesterase (CPD) component--that can function in tRNA splicing in vivo when expressed as separate polypeptides. To understand the structural requirements for the kinase-CPD domain, we performed an alanine scan of 30 amino acids that are conserved in Trl1 homologs from other fungi. We thereby identified four residues (Arg463, His515, Thr675 and Glu741) as essential for activity in vivo. Structure-function relationships at these positions, and at four essential or conditionally essential residues defined previously (Asp425, Arg511, His673 and His777), were clarified by introducing conservative substitutions. Biochemical analysis showed that lethal mutations of Asp425, Arg463, Arg511 and His515 in the kinase module abolished polynucleotide kinase activity in vitro. We report that a recently cloned 1104 amino acid Arabidopsis RNA ligase functions in lieu of yeast Trl1 in vivo and identify essential side chains in the ligase, kinase and CPD modules of the plant enzyme. The plant ligase, like yeast Trl1 but unlike T4 RNA ligase 1, requires a 2'-PO4 end for tRNA splicing in vivo.

Indexed as

RNA Splicing2',3'-Cyclic-Nucleotide PhosphodiesterasesAmino Acid SequenceArabidopsisArabidopsis ProteinsCatalytic DomainDNA Mutational AnalysisGenetic Complementation TestMolecular Sequence DataPlant ProteinsPolynucleotide 5'-Hydroxyl-KinaseRNA Ligase (ATP)RNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino Acid2',3'-Cyclic-Nucleotide PhosphodiesterasesArabidopsis ProteinsPlant ProteinsPolynucleotide 5'-Hydroxyl-KinaseRNA Ligase (ATP)RNA, TransferSaccharomyces cerevisiae ProteinsTrl1 protein, S cerevisiae

Identifiers

PMID16428247
PMCPMC1345694
OpenAlexW2113984566

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.