ISSN 10214437, Russian Journal of Plant Physiology, 2012, Vol. 59, No. 2, pp. 255–265. © Pleiades Publishing, Ltd., 2012.
Published in Fiziologiya Rastenii, 2012, Vol. 59, No. 2, pp. 284–293.
The 1433 proteins are a family of acidic soluble
proteins that were originally isolated from mammalian
brain tissue and named on the basis of chromatogra
phy elution and starchgel electrophoresis . Ini
tially, it was considered that 1433 proteins are spe
cific for mammalian brain tissue as they were found
there at high concentrations. Since then, 1433 pro
teins have been discovered in other eukaryotic species,
and now there is consensus that 1433 genes are
present in all eukaryotic organisms .
1433 proteins are conserved in their core
domains both within and across species and are highly
variable in their N and Cterminal domains. The
members of this protein family function as homo and
heterodimers, forming a clampshape structure. 1433
dimers are able to interact with either two different
This text was submitted by the authors in English.
phosphorylated targets, or bind one target at two positions.
Extensive studies resulted in the identification of three
peptide modes, commonly recognized by 1433s: mode I
), mode II
is an aromatic or aliphatic amino acid and X is
any amino acid) and a Cterminal mode III motif
COOH (where X denotes any amino acid
and pS/T denotes phosphoserine/threonine) .
Most proteins interacting with 1433s are phosphory
lated on Ser or Thr residues present in one of these
conserved motifs. However, not all the proteins that
interact with 1433s comprise these canonical
sequences. In addition, some motifs, like WLDLE and
GHSL, do not require phosphorylation to be recog
nized by 1433 proteins.
Recent studies using highthroughput techniques
like yeast twohybrid screening of a cDNA library,
affinity chromatography, and pulldown assay using
isoform specific antibodies or
Sequence Analysis and Expression Profiling of 1433 Genes
from the Extremophile
, Ecotype Yakutsk
D. A. Vysotskii
, M. B. Kostina
, T. Roslyakova
, T. Leonova
, E. Souer
A. V. Babakov
and A. H. de Boer
AllRussia Institute of Agricultural Biotechnology, Timiryazevskaya ul. 42, Moscow, 127550 Russia;
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences,
ul. MiklukhoMaklaya 16/10, Moscow, 117977 Russia
Department of Genetics, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1085,
1081 HV Amsterdam, The Netherlands
Department of Structural Biology, Faculty of Earth and Life Sciences, Vrije Universiteit,
De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands
Received April 19, 2011
—Members of the 1433 protein family are known to be important regulators of plant primary
metabolism, hormonal signal transduction, and ion homeostasis. We identified nine isoforms of 1433 genes
an extremophile relative of
All the identified isoforms were
designated according to their
orthologs: Chi, Omega, Psi, Phi, Upsilon, Lambda, Mu, Epsilon,
and Omicron. Comparison of the deduced amino acid sequences reveals high degree of identity between the
members of this protein family. Isoforms, designated as Ts1433 Chi, Omicron, and Mu, display noticeable
differences in their Cterminal domain as compared to their
homologs. Phylogenetic analysis
demonstrated that the identified isoforms split into two groups, epsilon and nonepsilon, according to the
common classification of the 1433 family genes. The
1433 isoforms are differentially
expressed in various plant tissues, and realtime RTPCR revealed that most of the isoforms are highly
expressed even under normal growth conditions. In response to abiotic stress, low temperatures and high con
centrations of salts, 1433 genes exhibited different expression patterns. Our data suggest that, due to the
high expression levels of the 1433 genes,
plants are likely preadapted to the stress conditions.
Differences between the Cterminal domains of some
1433 proteins and their
homologs may result in differences in target protein specificity.
, 1433 proteins, expression, realtime PCR.