Nuclear Protein-Only Ribonuclease P2 Structure and Biochemical Characterization Provide Insight into the Conserved Properties of tRNA 5′ End Processing Enzymes
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- 作者：Agnes Karasik1 ; Aranganathan Shanmuganathan1 ; Michael J. Howard2 ; Carol A. Fierke2 ; 3 ; Markos Koutmos1 ; markos.koutmos@usuhs.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：PRORP ; protein-only RNase P ; pre-tRNA ; precursor tRNA ; PPR ; pentatricopeptide repeat ; TCEP ; tris(2-carboxyethyl)phosphine ; EDTA ; ethylenediaminetetraacetic acid
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：16 January 2016
- 年：2016
- 卷：428
- 期：1
- 页码：26-40
- 全文大小：1197 K
文摘
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PRORPs were recently discovered in Eukaryotes.
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In vitro activity of nuclear PRORP2 is comparable to that of organellar PRORP1.
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Nuclear PRORP2 processes the mitochondrial pre-t-element slower.
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PRORP1 and PRORP2 have similar structures but are trapped in two different conformations.
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Nuclear and organellar PRORPs have conserved structural and functional properties.
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