Evidence map›Paper›PMID 17242192›Full record

ArticleMolecular and cellular biology2007

Swapping the gene-specific and regional silencing specificities of the Hst1 and Sir2 histone deacetylases.

Janet Mead, Ron McCord, Laura Youngster, Mandakini Sharma, Marc R Gartenberg, Andrew K Vershon

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Crystallization and preliminary crystallographic studies of the NAD+-dependent deacetylase HST1 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  7. Review
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  10. 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

6 authors at 1 institution in 1 country.

Janet MeadWaksman Institute, 190 Frelinghuysen Road, Piscataway, NJ 08854-8020, USA.
Ron McCord
Laura Youngster
Mandakini Sharma
Marc R Gartenberg
Andrew K Vershon
Rutgers, The State University of New Jersey · US

Funding

Cohesin in Chromosome Architecture and Transcriptional ControlR01GM051402 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GARTENBERG, MARC R. · 1995 to 2022
$7.9M
TRANSCRIPTIONAL REGULATION OF MEIOTIC GENES IN YEASTR01GM058762 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI VERSHON, ANDREW · 2000 to 2003
$799k
CHROMOSOME ARCHITECTURER55GM051402 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GARTENBERG, MARC R. · 1994 to 1994
–
NIGMS NIH HHS GM 51402NIGMS NIH HHS GM 58762NIGMS NIH HHS R01 GM051402NIGMS NIH HHS R01 GM058762
6 · The paper itself

Abstract

Sir2 and Hst1 are NAD(+)-dependent histone deacetylases of budding yeast that are related by strong sequence similarity. Nevertheless, the two proteins promote two mechanistically distinct forms of gene repression. Hst1 interacts with Rfm1 and Sum1 to repress the transcription of specific middle-sporulation genes. Sir2 interacts with Sir3 and Sir4 to silence genes contained within the silent-mating-type loci and telomere chromosomal regions. To identify the determinants of gene-specific versus regional repression, we created a series of Hst1::Sir2 hybrids. Our analysis yielded two dual-specificity chimeras that were able to perform both regional and gene-specific repression. Regional silencing by the chimeras required Sir3 and Sir4, whereas gene-specific repression required Rfm1 and Sum1. Our findings demonstrate that the nonconserved N-terminal region and two amino acids within the enzymatic core domain account for cofactor specificity and proper targeting of these proteins. These results suggest that the differences in the silencing and repression functions of Sir2 and Hst1 may not be due to differences in enzymatic activities of the proteins but rather may be the result of distinct cofactor specificities.

Indexed as

Gene SilencingAmino Acid SequenceCoenzymesDNA-Binding ProteinsHistone DeacetylasesMolecular Sequence DataNuclear ProteinsProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSilent Information Regulator Proteins, Saccharomyces cerevisiaeSirtuin 2SirtuinsCoenzymesDNA-Binding ProteinsHistone DeacetylasesHST1 protein, S cerevisiaeNuclear ProteinsRepressor ProteinsRfm1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR2 protein, S cerevisiaeSIR3 protein, S cerevisiaeSIR4 protein, S cerevisiaeSirtuin 2SirtuinsSUM1 protein, S cerevisiae

Identifiers

PMID17242192
PMCPMC1899883
OpenAlexW2115631584

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.