Molecular mechanisms of a multifunctional AAA protein, p97

P97是许多细胞过程所需的必需AAA ATP酶，并且被鉴定为常染色体显性人类疾病、与骨的佩吉特病相关的包涵体肌病和额颞痴呆的致病基因。P97具有两个AAA结构域，其中与疾病相关的突变大多发现于N-末端的一半。在这项研究中，在每个AAA结构域的ATP酶活性缺陷的突变酵母p97的功能的影响进行了分析。在该结果中，发现C-末端AAA结构域对于p97功能是必需的，其由N-末端AAA结构域调制。

P97 is an essential AAA ATPase that is required for many cellular processes, and is identified as a causative gene for an autosomal dominant human disorder, inclusion body myopathy associated with Paget's disease of the bone and frontotemporal dementia. P97 possesses two AAA domains, in which disease-related mutations are mostly found in the N-terminal half. In this study, effects of mutations defective in ATPase activity in each AAA domain on the function of yeast p97 were analyzed. In this result, it is found that the C-terminal AAA domain is essential for p97 functions, which is modulated by the N-terminal AAA domain.