Journal
CELL STRESS & CHAPERONES
Volume 26, Issue 1, Pages 265-274Publisher
SPRINGER
DOI: 10.1007/s12192-020-01156-3
Keywords
Small heat shock protein (sHsp); DmHsp27; Chaperone; Alpha-crystallin domain (ACD); Drosophila melanogaster; Insect
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Through sequence analysis, 56 additional insect sHsps with conserved nuclear localization signals were identified. The exact role of nuclear sHsps remains unknown, but DmHsp27 may have roles in molecular chaperoning and other nuclear processes such as chromatin remodeling and transcription. Identification of DmHsp27 interactors could provide insights into the cellular and molecular functions of this nuclear chaperone.
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.
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