期刊
CELL STRESS & CHAPERONES
卷 26, 期 1, 页码 265-274出版社
SPRINGER
DOI: 10.1007/s12192-020-01156-3
关键词
Small heat shock protein (sHsp); DmHsp27; Chaperone; Alpha-crystallin domain (ACD); Drosophila melanogaster; Insect
类别
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据