Analysis of insect nuclear small heat shock proteins and interacting proteins

被引:7
|
作者
Moutaoufik, Mohamed Taha [1 ,2 ]
Tanguay, Robert M. [1 ]
机构
[1] Univ Laval, Med Sch, Dept Cellular & Mol Biol Med Biochem & Pathol, Lab Cell & Dev Genet, Quebec City, PQ G1K 7P4, Canada
[2] Univ Regina, Dept Biochem, Regina, SK S4S 0A2, Canada
来源
CELL STRESS & CHAPERONES | 2021年 / 26卷 / 01期
关键词
Small heat shock protein (sHsp); DmHsp27; Chaperone; Alpha-crystallin domain (ACD); Drosophila melanogaster; Insect; ALPHA-B-CRYSTALLIN; ARABIDOPSIS-THALIANA; NEURONAL EXPRESSION; LOCALIZATION SIGNAL; FUNCTIONAL-ANALYSIS; DROSOPHILA HOMOLOG; STRESS PROTEINS; CELL; HSP27; GENE;
D O I
10.1007/s12192-020-01156-3
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The small heat shock proteins (sHsps) are a ubiquitous family of ATP-independent stress proteins found in all domains of life.Drosophila melanogasterHsp27 (DmHsp27) is the only known nuclear sHsp in insect. Here analyzing sequences from HMMER, we identified 56 additional insect sHsps with conserved arginine-rich nuclear localization signal (NLS) in the N-terminal region. At this time, the exact role of nuclear sHsps remains unknown. DmHsp27 protein-protein interaction analysis from iRefIndex database suggests that this protein, in addition to a putative role of molecular chaperone, is likely involved in other nuclear processes (i.e., chromatin remodeling and transcription). Identification of DmHsp27 interactors should provide key insights on the cellular and molecular functions of this nuclear chaperone.
引用
收藏
页码:265 / 274
页数:10
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