Evidence map›Paper›PMID 15902492›Full record

ArticleMolecular genetics and genomics : MGG2005

The Elp3 subunit of human Elongator complex is functionally similar to its counterpart in yeast.

Fen Li, Jun Lu, Qiuju Han, Guoping Zhang, Baiqu Huang

Abstract read
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In one paragraph

Article in Molecular genetics and genomics : MGG, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The Many Faces of Elongator in Neurodevelopment and Disease.Frontiers in molecular neuroscience · 2016
    Review
  8. Dimerization of elongator protein 1 is essential for Elongator complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Fen LiInstitute of Genetics and Cytology, Northeast Normal University, Changchun 130024, PR China.
Jun Lu
Qiuju Han
Guoping Zhang
Baiqu Huang
Northeast Normal University · CNHenan Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functions of the Elp3 subunit of the recently purified human Elongator were studied using an in vivo yeast complementation system. We demonstrated that the human ELP3 gene (hELP3) was able partially to complement functional defects of yeast elp3Delta cells. Furthermore, a chimeric ELP3 gene (yhELP3) encoding a protein in which the putative histone acetyltransferase (HAT) domain of hELP3 fused to the remainder of the yeast Elp3p corrected the growth defects of elp3Delta cells and complemented the slow activation of some inducible genes. Moreover, deletion of the B motif of the catalytic domain of the HAT region of hELP3 eliminated the ability of yhELP3 to complement elp3Delta in vivo, indicating that the HAT activity is essential for ELP3 function. We also demonstrated that replacement of specific lysine residues in histones H3 and H4 by arginine affected the complementation capacity of both the yeast gene (yELP3) and the chimeric yhELP3 in the elp3Deltastrain. Specifically, mutation of lysine-14 of H3 (H3 K14R) or lysine-8 of H4 (H4 K8R) reduced the ability of yELP3 and yhELP3 to complement the elp3Delta mutant, whereas simultaneous mutation of both sites (H3 K14R/H4 K8R) almost completely abolished complementation. These results imply a link between the acetylation of specific sites in nucleosomal histones and the regulation of transcription elongation by human Elp3. The data presented in this report suggest that the Elp3 subunits of human and yeast are highly conserved in their structure and functions.

Indexed as

AcetyltransferasesBase SequenceDNA PrimersHistone AcetyltransferasesHumansMutagenesisPhenotypePlasmidsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSaccharomyces cerevisiaeAcetyltransferasesDNA PrimersHistone AcetyltransferasesRNA, Messenger

Identifiers

PMID15902492
OpenAlexW2007208925

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.