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 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.

小热休克蛋白 (sHsps) 是一个普遍存在的不依赖 ATP 的应激蛋白家族，存在于生命的所有领域。黑腹果蝇Hsp27 (DmHsp27) 是昆虫中唯一已知的核 sHsp。在这里分析来自 HMMER 的序列，我们确定了 56 个额外的昆虫 sHsps，在 N 端区域具有保守的富含精氨酸的核定位信号 (NLS)。目前，核 sHsps 的确切作用仍然未知。来自 iRefIndex 数据库的 DmHsp27 蛋白质-蛋白质相互作用分析表明，除了分子伴侣的假定作用外，该蛋白质还可能参与其他核过程（即染色质重塑和转录）。DmHsp27 相互作用子的鉴定应该提供关于这种核伴侣的细胞和分子功能的关键见解。