Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2.
Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2.
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DOI：
10.1186/1471-2148-10-272
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发表时间：
2010-09-06
影响因子：
3.4
通讯作者：
Huang Y
中科院分区：
文献类型：
--
作者：
Zhao W;Yu H;Li S;Huang Y
tRNase Z是负责tRNA前体的3 '-末端加工的核酸内切酶，这是tRNA 3'-CCA添加和随后的tRNA氨酰化所必需的过程。根据其大小，tRNase Z可以分为长（tRNase ZL）和短（tRNase ZS）形式。tRNase ZL被认为是由tRNase ZS的串联基因复制产生的，具有进一步的序列差异。tRNase Z的种类分布复杂。真菌是真核生物中进化上多样化的一类。真菌基因组序列的最近增殖提供了一个机会，探索真核生物tRNase Z的结构和功能的多样性。我们报告了84个完整的真菌基因组中候选tRNase Z的调查和分析，涵盖了广泛的真菌多样性。我们发现，tRNase ZL是存在于所有的真菌，我们已经检查，而tRNase ZS只存在于真菌门Basidiomycota，壶菌和接合菌。此外，我们发现，不像盘菌亚门和裂殖菌亚门，其中含有一个单一的tRNase ZL，裂殖酵母分裂酵母（Taphrinomycotina）含有两个tRNase ZL基因编码的两个tRNase ZL。这两个tRNase ZL最有可能分别定位于细胞核和线粒体，表明在裂变酵母中两个不同tRNase ZL之间的tRNase Z功能的分配。真菌tRNase Z基因发生表明，tRNase ZLs是tRNase ZLs的祖先。此外，真菌tRNase ZL的进化关系通常与真菌物种之间的已知系统发育关系一致，并支持某些真菌分类群（包括裂殖酵母）中的tRNase ZL基因复制。tRNase Z蛋白序列的分析揭示了大多数真菌tRNase ZLs和真菌tRNase ZLs亚组中假定的非典型底物结合结构域。最后，我们证明了伪底物识别和催化基序的存在下，在N-末端的tRNase ZLs的一半。本研究描述了候选真菌tRNase Z的首次全面鉴定和序列分析。我们的研究结果支持的建议，tRNase ZL已经演变为tRNase ZS基因的重复和多样化的结果。
tRNase Z is the endonuclease that is responsible for the 3'-end processing of tRNA precursors, a process essential for tRNA 3'-CCA addition and subsequent tRNA aminoacylation. Based on their sizes, tRNase Zs can be divided into the long (tRNase ZL) and short (tRNase ZS) forms. tRNase ZL is thought to have arisen from a tandem gene duplication of tRNase ZS with further sequence divergence. The species distribution of tRNase Z is complex. Fungi represent an evolutionarily diverse group of eukaryotes. The recent proliferation of fungal genome sequences provides an opportunity to explore the structural and functional diversity of eukaryotic tRNase Zs. We report a survey and analysis of candidate tRNase Zs in 84 completed fungal genomes, spanning a broad diversity of fungi. We find that tRNase ZL is present in all fungi we have examined, whereas tRNase ZS exists only in the fungal phyla Basidiomycota, Chytridiomycota and Zygomycota. Furthermore, we find that unlike the Pezizomycotina and Saccharomycotina, which contain a single tRNase ZL, Schizosaccharomyces fission yeasts (Taphrinomycotina) contain two tRNase ZLs encoded by two different tRNase ZL genes. These two tRNase ZLs are most likely localized to the nucleus and mitochondria, respectively, suggesting partitioning of tRNase Z function between two different tRNase ZLs in fission yeasts. The fungal tRNase Z phylogeny suggests that tRNase ZSs are ancestral to tRNase ZLs. Additionally, the evolutionary relationship of fungal tRNase ZLs is generally consistent with known phylogenetic relationships among the fungal species and supports tRNase ZL gene duplication in certain fungal taxa, including Schizosaccharomyces fission yeasts. Analysis of tRNase Z protein sequences reveals putative atypical substrate binding domains in most fungal tRNase ZSs and in a subset of fungal tRNase ZLs. Finally, we demonstrate the presence of pseudo-substrate recognition and catalytic motifs at the N-terminal halves of tRNase ZLs. This study describes the first comprehensive identification and sequence analysis of candidate fungal tRNase Zs. Our results support the proposal that tRNase ZL has evolved as a result of duplication and diversification of the tRNase ZS gene.
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影响因子：
10.7
作者：
Castresana, J
通讯作者：
Castresana, J
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作者：
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通讯作者：
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