Evidence map›Paper›PMID 17224141›Full record

ArticleDevelopmental biology2007

C2H2 zinc finger-SET histone methyltransferase is a plant-specific chromatin modifier.

Alexander Krichevsky, Helen Gutgarts, Stanislav V Kozlovsky, Tzvi Tzfira, Ann Sutton, Rolf Sternglanz, Gail Mandel, Vitaly Citovsky

Open access · greenAbstract readComparative Study
In one paragraph

Article in Developmental biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 66 citations in OpenAlex.

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  6. The function of histone lysine methylation related SET domain group proteins in plants.Protein science : a publication of the Protein Society · 2020
    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

8 authors at 2 institutions in 1 country.

Alexander KrichevskyDepartment of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794-5215, USA. akrichevsky@notes.cc.sunysb.edu
Helen Gutgarts
Stanislav V Kozlovsky
Tzvi Tzfira
Ann Sutton
Rolf Sternglanz
Gail Mandel
Vitaly Citovsky
State University of New York · USUniversity of Michigan · US

Funding

TRANSPORT THROUGH PLASMODESMATAR01GM050224 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI CITOVSKY, VITALY H · 1994 to 2020
$5.7M
PROTEINS AND ENZYMES AFFECTING CHROMATINR01GM028220 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI STERNGLANZ, ROLF · 1985 to 2006
$2.4M
Proteins and Enzymes Affecting ChromatinR56GM028220 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI STERNGLANZ, ROLF · 2007 to 2007
$387k
NIGMS NIH HHS GM 28220NIGMS NIH HHS R01 GM028220NIGMS NIH HHS R01 GM050224NIGMS NIH HHS R56 GM028220
6 · The paper itself

Abstract

Histone modification represents a universal mechanism for regulation of eukaryotic gene expression underlying diverse biological processes from neuronal gene expression in mammals to control of flowering in plants. In animal cells, these chromatin modifications are effected by well-defined multiprotein complexes containing specific histone-modifying activities. In plants, information about the composition of such co-repressor complexes is just beginning to emerge. Here, we report that two Arabidopsis thaliana factors, a SWIRM domain polyamine oxidase protein, AtSWP1, and a plant-specific C2H2 zinc finger-SET domain protein, AtCZS, interact with each other in plant cells and repress expression of a negative regulator of flowering, FLOWERING LOCUS C (FLC) via an autonomous, vernalization-independent pathway. Loss-of-function of either AtSWP1 or AtCZS results in reduced dimethylation of lysine 9 and lysine 27 of histone H3 and hyperacetylation of histone H4 within the FLC locus, in elevated FLC mRNA levels, and in moderately delayed flowering. Thus, AtSWP1 and AtCZS represent two main components of a co-repressor complex that fine tunes flowering and is unique to plants.

Indexed as

Gene Expression Regulation, PlantAmino Acid SequenceArabidopsisArabidopsis ProteinsChromatinChromatin ImmunoprecipitationDNA PrimersFlowersHistone-Lysine N-MethyltransferaseHistone MethyltransferasesMADS Domain ProteinsMicroarray AnalysisMolecular Sequence DataProtein MethyltransferasesReverse Transcriptase Polymerase Chain ReactionSequence AlignmentArabidopsis ProteinsAt5g10140 protein, ArabidopsisChromatinDNA PrimersHistone-Lysine N-MethyltransferaseHistone MethyltransferasesMADS Domain ProteinsProtein MethyltransferasesSTRUWWELPETER protein, Arabidopsis

Identifiers

PMID17224141
PMCPMC1831845
OpenAlexW1993020640

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.