Two variants of MutS homolog hMSH5: prevalence in humans and effects on protein interaction.
Two variants of MutS homolog hMSH5: prevalence in humans and effects on protein interaction.
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DOI：
10.1016/j.bbrc.2005.04.154
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发表时间：
2005-07
影响因子：
3.1
通讯作者：
Wei Yi;Xiling Wu;Tai-Hsien Lee;N. Doggett;C. Her
中科院分区：
文献类型：
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作者：
Wei Yi;Xiling Wu;Tai-Hsien Lee;N. Doggett;C. Her
已知MSH5在一系列细胞过程中发挥功能作用，如DNA损伤反应和减数分裂同源重组。在这里，我们报道了一种hMSH5剪接变体（hMSH5sv）的特征，它是由hMSH5内含子6最后51bp的保留引起的，其中编码的17个氨基酸插入密码子179和180之间并不影响其与hMSH4相互作用的能力。我们还发现了一个hMSH5多态性（C84T），它改变了hMSH5基因的密码子29，导致脯氨酸到丝氨酸的变化（P29S）。确定了hMSH4和hMSH5的相互作用域。P29S的改变位于相互作用域内，导致蛋白与hMSH4的相互作用减弱。总之，我们目前的研究揭示了人类细胞中存在两种形式的hMSH5变体。与这两种hMSH5变体相关的不同特性强调了人类hMSH5基因潜在的功能多样性。
MSH5 is known to play functional roles in an array of cellular processes such as DNA damage response and meiotic homologous recombination. Here, we report the characterization of an hMSH5 splicing variant (hMSH5sv) that resulted from the retention of the last 51bp of hMSH5 intron 6, in which the encoded 17-amino acid insertion between codons 179 and 180 does not compromise its capability to interact with hMSH4. We have also identified an hMSH5 polymorphism (C84T) that altered codon 29 of the hMSH5 gene resulting in a proline-to-serine change (P29S). The interaction domains of hMSH4 and hMSH5 have also been resolved. The P29S alteration is located within the interacting domain and leads to a weakened protein interaction with hMSH4. Together, our present study revealed the existence of two forms of hMSH5 variants in human cells. The different properties associated with these two hMSH5 variants underscore the potential functional diversity of the human hMSH5 gene.