Evidence map›Paper›PMID 21051361›Full record

ArticleNucleic acids research2011

tRNA 5'-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea.

Bhalchandra S Rao, Emily L Maris, Jane E Jackman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. A comparison ofbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

3 authors at 2 institutions in 1 country.

Bhalchandra S RaoDepartment of Biochemistry and Center for RNA Biology and Molecular, Cellular and Developmental Biology Graduate Program, The Ohio State University, Columbus, OH 43210, USA.
Emily L Maris
Jane E Jackman
Center for Excellence in Education · USThe Ohio State University · US

Funding

Molecular Mechanism and Biological Function of 3'-5' PolymerasesR01GM087543 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH · 2010 to 2019
$2.7M
NIGMS NIH HHS GM087543NIGMS NIH HHS R01 GM087543
6 · The paper itself

Abstract

The tRNA(His) guanylyltransferase (Thg1) family comprises a set of unique 3'-5' nucleotide addition enzymes found ubiquitously in Eukaryotes, where they function in the critical G(-1) addition reaction required for tRNA(His) maturation. However, in most Bacteria and Archaea, G(-1) is genomically encoded; thus post-transcriptional addition of G(-1) to tRNA(His) is not necessarily required. The presence of highly conserved Thg1-like proteins (TLPs) in more than 40 bacteria and archaea therefore suggests unappreciated roles for TLP-catalyzed 3'-5' nucleotide addition. Here, we report that TLPs from Bacillus thuringiensis (BtTLP) and Methanosarcina acetivorans (MaTLP) display biochemical properties consistent with a prominent role in tRNA 5'-end repair. Unlike yeast Thg1, BtTLP strongly prefers addition of missing N(+1) nucleotides to 5'-truncated tRNAs over analogous additions to full-length tRNA (k(cat)/K(M) enhanced 5-160-fold). Moreover, unlike for -1 addition, BtTLP-catalyzed additions to truncated tRNAs are not biased toward addition of G, and occur with tRNAs other than tRNA(His). Based on these distinct biochemical properties, we propose that rather than functioning solely in tRNA(His) maturation, bacterial and archaeal TLPs are well-suited to participate in tRNA quality control pathways. These data support more widespread roles for 3'-5' nucleotide addition reactions in biology than previously expected.

Indexed as

Bacillus thuringiensisGenetic Complementation TestKineticsMethanosarcinaNucleotidesNucleotidyltransferasesRNA, Transfer, HisRNA, Transfer, PheYeastsguanylyltransferaseNucleotidesNucleotidyltransferasesRNA, Transfer, HisRNA, Transfer, Phe

Identifiers

PMID21051361
PMCPMC3061083
OpenAlexW2079386209

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.