

Author: Taranov V. Berdnikova M. Nosov A. Galkin A. Babakov A.
Publisher: MAIK Nauka/Interperiodica
ISSN: 0026-8933
Source: Molecular Biology, Vol.44, Iss.5, 2010-10, pp. : 787-794
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
Four genes encoding cold shock domain (CSD) proteins have been identified in salt cress Thellungiella salsuginea (halophila), an extremophyte currently recognized as a promising model for studying stress tolerance]. The deduced proteins prove highly homologous to those of Arabidopsis thaliana (up to 95% identity) and are accordingly enumerated TsCSDP1-TsCSDP4; after the N-proximal conserved CSD, they have respectively 6, 2, 7, and 2 zinc finger motifs evenly spaced by Gly-rich stretches. Much lower similarity (∼45%) is observed in the regions upstream of TATA-box promoters of TsCSDP1 vs. AtCSP1, with numerous distinctions in the sets of identifiable cis-regulatory elements. Plasmid expression of TsCSDP1 (like AtCSP1/3) rescues a cold-sensitive csp-lacking mutant of Escherichia coli, confirming that the protein is functional. In leaves of salt cress plants under normal conditions, the mRNA levels for the four TsCSDPs relate as 10: 27: 1: 31. Chilling to 4°C markedly alters the gene expression; the 4-day dynamics are different for all four genes and quite dissimilar from those reported for their Arabidopsis homologous under comparable conditions. Thus, the much greater cold hardiness of Thellungiella vs. Arabidopsis cannot be explained by structural distinctions of its CSDPs, but rather may be due to expedient regulation of their expression at low temperature.
Related content




A superfamily of proteins that contain the cold-shock domain
By Graumann P.L. Marahiel M.A.
Trends in Biochemical Sciences, Vol. 23, Iss. 8, 1998-08 ,pp. :


By Kim Jin Sun Park Su Jung Kwak Kyung Jin Kim Yeon Ok Kim Joo Yeol Song Jinkyung Jang Boseung Jung Che-Hun Kang Hunseung
Nucleic Acids Research, Vol. 35, Iss. 2, 2007-01 ,pp. :

