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首页> 外文期刊>BMC Genomics >Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein
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Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein

机译：Midasin的表达和基因组分析，Mindasin是一种与动力蛋白遥遥相关的新型且高度保守的AAA蛋白

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Background The largest open reading frame in the Saccharomyces genome encodes midasin (MDN1p, YLR106p), an AAA ATPase of 560 kDa that is essential for cell viability. Orthologs of midasin have been identified in the genome projects for Drosophila, Arabidopsis, and Schizosaccharomyces pombe. Results Midasin is present as a single-copy gene encoding a well-conserved protein of ~600 kDa in all eukaryotes for which data are available. In humans, the gene maps to 6q15 and encodes a predicted protein of 5596 residues (632 kDa). Sequence alignments of midasin from humans, yeast, Giardia and Encephalitozoon indicate that its domain structure comprises an N-terminal domain (35 kDa), followed by an AAA domain containing six tandem AAA protomers (~30 kDa each), a linker domain (260 kDa), an acidic domain (~70 kDa) containing 35–40% aspartate and glutamate, and a carboxy-terminal M-domain (30 kDa) that possesses MIDAS sequence motifs and is homologous to the I-domain of integrins. Expression of hemagglutamin-tagged midasin in yeast demonstrates a polypeptide of the anticipated size that is localized principally in the nucleus. Conclusions The highly conserved structure of midasin in eukaryotes, taken in conjunction with its nuclear localization in yeast, suggests that midasin may function as a nuclear chaperone and be involved in the assembly/disassembly of macromolecular complexes in the nucleus. The AAA domain of midasin is evolutionarily related to that of dynein, but it appears to lack a microtubule-binding site.
机译：背景酿酒酵母基因组中最大的开放阅读框编码Midasin（MDN1p，YLR106p），这是一种560 kDa的AAA ATPase，对细胞活力至关重要。在果蝇，拟南芥和粟酒裂殖酵母的基因组计划中已经确定了Midasin的直系同源物。结果Midasin以单拷贝基因的形式存在，在所有可获得数据的真核生物中均编码约600 kDa的保守蛋白。在人类中，该基因定位于6q15，并编码5596个残基的预测蛋白质（632 kDa）。来自人类，酵母，贾第鞭毛虫和脑脊髓炎的Midasin的序列比对表明，其结构域结构包含一个N端结构域（35 kDa），其后是一个包含六个串联AAA启动子的AAA结构域（每个约30 kDa），一个连接子结构域（260个） kDa），包含35-40％的天冬氨酸和谷氨酸的酸性结构域（约70 kDa），以及具有MIDAS序列基序且与整联蛋白I结构域同源的羧基末端M结构域（30 kDa）。酵母中带有血凝素标记的Midasin的表达表明，预期大小的多肽主要位于细胞核中。结论真核生物中米达辛的高度保守结构与其在酵母中的核定位相结合，表明米达辛可能起核分子伴侣的作用，并参与细胞核中大分子复合物的组装/拆卸。 Midasin的AAA结构域与Dynein的进化相关，但似乎缺乏微管结合位点。

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