Analysis of insect nuclear small heat shock proteins and interacting proteins
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Analysis of insect nuclear small heat shock proteins and interacting proteins Mohamed Taha Moutaoufik 1,2 & Robert M. Tanguay 1 Received: 7 June 2020 / Revised: 13 August 2020 / Accepted: 19 August 2020 # Cell Stress Society International 2020
Abstract The small heat shock proteins (sHsps) are a ubiquitous family of ATP-independent stress proteins found in all domains of life. Drosophila melanogaster Hsp27 (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 Nterminal 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. Keywords Small heat shock protein (sHsp) . DmHsp27 . Chaperone . Alpha-crystallin domain (ACD) . Drosophila melanogaster . Insect
Introduction The nucleus is the cellular organelle that distinguishes eukaryotes from prokaryotes. A large number of biological activities occur in the nucleus, including DNA replication and damage repair, the biogenesis of ribosomal RNA precursors, transcription, and splicing of pre-mRNAs. Many proteins are involved in nuclear transport in processes dependent on Karyopherin-β proteins (both importins and exportins). The small heat shock proteins (sHsps) are a ubiquitous family of ATP-independent stress proteins found in all domains of life (Caspers et al. 1995; de Jong et al. 1998; Fu et al. 2006; Maaroufi and Tanguay 2013). These proteins are upregulated in response to a variety of stresses that negatively Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12192-020-01156-3) contains supplementary material, which is available to authorized users. * Robert M. Tanguay [email protected] 1
Lab of Cell & Developmental Genetics, Department of Cellular and Molecular Biology, Medical Biochemistry & Pathology, Medical School, Université Laval, Quebec G1K 7P4, Canada
2
Present address: Department of Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada
impact protein homeostasis. sHsp sequence analysis indicates a tripartite architecture, with a conserved α-crystallin domain (ACD) flanked by a variable non-conserved N- and Cterminal regions (NTR and CTR) (Kappé et al. 2010; Basha et al. 2012). sHsp number, level and stage of expression, tissue distribution, and intracellular localization can show differences between species, suggesting that sHsps have adapted to their environment and to specific cell needs (Michaud et al. 2002; Morrow and Tanguay 2015). Relocation of cytosolic sHsps to the nucleus is observed under certain conditions of stress in virtually
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