Evidence map›Paper›PMID 16908543›Full record

ArticleMolecular and cellular biology2006

Sir3 C-terminal domain involvement in the initiation and spreading of heterochromatin.

Hungjiun Liaw, Arthur J Lustig

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  13. Chromatin higher-order structure and dynamics.Cold Spring Harbor perspectives in biology · 2010
    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

2 authors at 1 institution in 1 country.

Hungjiun LiawDepartment of Biochemistry, Tulane University Health Sciences Center, 1430 Tulane Avenue, New Orleans, LA 70112, USA.
Arthur J Lustig
Tulane University · US

Funding

Eukaryotic Telomere DynamicsR01GM069943 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI LUSTIG, ARTHUR J. · 2004 to 2014
$2.7M
Eukaryotic Telomere DynamicsR56GM069943 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI LUSTIG, ARTHUR J. · 2009 to 2009
$345k
NIGMS NIH HHS GM 069943NIGMS NIH HHS R01 GM069943NIGMS NIH HHS R56 GM069943
6 · The paper itself

Abstract

Heterochromatin is nucleated at a specific site and subsequently spreads into distal sequences through multiple interactions between modified histones and nonhistone proteins. In the yeast Saccharomyces cerevisiae, these nonhistone proteins include Sir2, Sir3, and Sir4. We have previously shown that loss of the C-terminal Rap1 domain containing Sir3 and Sir4 association sites can be overcome by tethering a 144-amino-acid C-terminal domain (CTD) of Sir3 adjacent to the telomere. Here, we explore the substructure and functions of the CTD. We demonstrate that the CTD is the minimum domain for Sir3 homodimerization, a function that is conserved in related yeasts. However, CTD heterodimers associate at only low efficiencies and correspondingly have low levels of tethered silencing, consistent with an essential role for dimerization in tethered silencing. Six missense alleles were generated, with ctd-Y964A producing the most extreme phenotypes when tethered to the LexA binding sites. Although ctd-Y964A is capable of dimerization, telomere silencing is abrogated, indicating that the CTD serves a second essential function in silencing. Chromatin immunoprecipitation analyses of wild-type and ctd-Y964A mutant cells indicate an association of the CTD with the deacetylated histone tails of H3 and H4 that is necessary for the recruitment of Sir3. The efficiency of spreading depends upon the apparent stoichiometry and stability during the initiation event. The predicted Cdc6 domain III winged-helix structure may well be responsible for dimerization.

Indexed as

Binding SitesChromatinComputational BiologyDimerizationGene SilencingHeterochromatinHistonesModels, MolecularMutationPhylogenyProtein Structure, TertiarySaccharomyces cerevisiaeSerine EndopeptidasesSilent Information Regulator Proteins, Saccharomyces cerevisiaeStructural Homology, ProteinTelomereChromatinHeterochromatinHistonesSerine EndopeptidasesSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR3 protein, S cerevisiae

Identifiers

PMID16908543
PMCPMC1636858
OpenAlexW2148817601

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.