The PUB domain: A putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway
The PUB domain: A putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway
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DOI：
10.1006/bbrc.2001.5688
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发表时间：
2001-10-12
影响因子：
3.1
通讯作者：
Lennarz, WJ
中科院分区：
文献类型：
--
作者：
Suzuki, T;Park, H;Lennarz, WJ
细胞质肽：N-聚糖酶（PNGase）是一种去N-糖基化酶，可能参与蛋白酶体依赖性途径，降解内质网（ER）中形成的错误折叠糖蛋白，并将其输出到细胞质中。在酿酒酵母中发现的细胞质PNGase Png 1 p广泛分布于高等真核生物以及酵母中（Suzuki，T.，等人，J. Cell Biol.149，1039-1051，2000）。最近发现的拟南芥全基因组序列促使我们在这种生物体中寻找Png 1 p的蛋白质同源物。有趣的是，当小鼠Png 1 p同源序列被用作查询时，不仅鉴定出含有被认为含有PNGase活性催化三联体的转氨酶样结构域的Png 1 p同源物，而且鉴定出具有长度为46个氨基酸的结构域的四种蛋白质，其与小鼠Png 1 p的N-末端表现出显著的相似性。此外，还发现这些同源蛋白中的三个具有乌巴或UBX结构域，其存在于参与泛素相关途径的各种蛋白中。我们命名这个新发现的同源区域的PUB（肽：N-聚糖酶/乌巴或UBX含蛋白）结构域，并提出，该结构域可能介导蛋白质-蛋白质相互作用。(C)北京：科学出版社.
Cytoplasmic peptide:N-glycanase (PNGase) is a de-N-glycosylating enzyme which may be involved in the proteasome-dependent pathway for degradation of misfolded glycoproteins formed in the endoplasmic reticulum (ER) that are exported into the cytoplasm. A cytoplasmic PNGase found in Saccharomyces cerevisiae, Png1p, is widely distributed in higher eukaryotes as well as in yeast (Suzuki, T., et al. J. Cell Biol. 149, 1039-1051, 2000). The recently uncovered complete genome sequence of Arabidopsis thaliana prompted us to search for the protein homologue of Png1p in this organism. Interestingly, when the mouse Png1p homologue sequence was used as a query, not only a Png1p homologue containing a transglutaminase-like domain that is believed to contain a catalytic triad for PNGase activity, but also four proteins which had a domain of 46 amino acids in length that exhibited significant similarity to the N-terminus of mouse Png1p were identified. Moreover, three of these homologous proteins were also found to possess a UBA or UBX domain, which are found in various proteins involved in the ubiquitin-related pathway. We name this newly found homologous region the PUB (Peptide:N-glycanase/UBA or UBX-containing proteins) domain and propose that this domain may mediate protein-protein interactions. (C) 2001 Academic Press.