National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Bioinformatics. 2010 Jan 15;26(2):149-52. doi: 10.1093/bioinformatics/btp647. Epub 2009 Nov 17.
Using sensitive sequence profile analysis, we identify a hitherto uncharacterized cysteine-rich, transmembrane (TM) module, CYSTM, found in a wide range of tail-anchored membrane proteins across eukaryotes. This superfamily includes Schizosaccharomyces Uvi15, Arabidopsis PCC1, Digtaria CDT1 and Saccharomyces proteins YDL012C and YDR210W, which have all been implicated in resistance/response to stress or pathogens. Based on the pattern of conserved cysteines and data from different chemical genetics studies, we suggest that CYSTM proteins might have critical role in responding to deleterious compounds at the plasma membrane via chelation or redox-based mechanisms. Thus, CYSTM proteins are likely to be part of a novel cellular protective mechanism that is widely active in eukaryotes, including humans.
Supplementary data are available at Bioinformatics online.
利用敏感序列图谱分析,我们鉴定了一个此前未被描述的富含半胱氨酸、跨膜(TM)模块 CYSTM,该模块存在于真核生物中广泛的尾部锚定膜蛋白中。这个超家族包括酿酒酵母 Uvi15、拟南芥 PCC1、大黍 CDT1 和酿酒酵母蛋白 YDL012C 和 YDR210W,它们都被牵连到对压力或病原体的抵抗/反应中。基于保守半胱氨酸的模式和来自不同化学遗传学研究的数据,我们推测 CYSTM 蛋白可能在通过螯合或基于氧化还原的机制来响应质膜上的有害化合物方面发挥关键作用。因此,CYSTM 蛋白可能是一种广泛存在于真核生物(包括人类)中的新型细胞保护机制的一部分。
补充数据可在“Bioinformatics”在线获取。