Evidence map›Paper›PMID 21750977›Full record

ArticleMolecular and cellular biochemistry2011

Specific characteristics of CK2β regulatory subunits in plants.

Isabel Cristina Velez-Bermudez, Sami Irar, Lorenzo Carretero-Paulet, Montserrat Pagès, Marta Riera

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Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Crystal structure of Arabidopsis thaliana casein kinase 2 α1.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Isabel Cristina Velez-BermudezMolecular Genetics Department, Centre for Research on Agricultural Genomics CRAG, Campus UAB 08193 Bellaterra, Cerdanyola del Vallès, Barcelona, Spain.
Sami Irar
Lorenzo Carretero-Paulet
Montserrat Pagès
Marta Riera

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In all eukaryotes, the typical CK2 holoenzyme is an heterotetramer composed of two catalytic (CK2α and CK2α') and two regulatory (CK2β) subunits. One of the distinctive traits of plant CK2 is that they present a greater number of genes encoding for CK2α/β subunits than animals or yeasts, for instance, in Arabidopsis and maize both CK2α/β subunits belong to multigenic families composed by up to four genes. Here, we conducted a genome-wide survey examining 34 different plant genomes in order to investigate if the multigenic property of CK2β genes is a common feature through the entire plant kingdom. Also, at the level of structure, the plant CK2β regulatory subunits present distinctive features as (i) they lack about 20 aminoacids in the C-terminal domain, (ii) they present a specific N-terminal extension of about 90 aminoacids that shares no homology with any previously characterized functional domain, and (iii) the acidic loop region is poorly conserved at the aminoacid level. Since there is no data about CK2β or holoenzyme structure in plants, in this study, we use human CK2β as a template to predict a structure for Zea mays CK2β1 by homology modeling and we discuss about possible structural changes in the acidic loop region that could affect the enzyme regulation.

Indexed as

Amino Acid SequenceCasein Kinase IIGenes, PlantHumansMolecular Sequence DataSequence AlignmentStructural Homology, ProteinZea maysCasein Kinase II

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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.