Purification and characterization of RNase P from Clostridium sporogenes.
Purification and characterization of RNase P from Clostridium sporogenes.
复制标题
产孢梭菌 RNase P 的纯化和表征。
DOI:
10.1111/j.1365-2958.1990.tb00718.x
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发表时间:
1990
影响因子:
3.6
通讯作者:
Marsh,TL
中科院分区:
文献类型:
--
作者:
Roselli,DM;Marsh,TL
RNase P is a multi‐subunit enzyme responsible for the accurate processing of the 5′ terminus of all tRNAs. The RNA subunit fromClostridium sporogeneshas been partially purified and characterized. The RNA is approximately 400 nucleotides long and makes a precise endonucleolytic cleavage at the mature 5′ terminus of tRNA. The RNA requires moderate concentrations of Mg2+(20mM) and relatively high concentrations of NH4Cl (800mM) for optimal activity. Mn2+effectively substitutes for Mg2+at 2mM. Zn2+, Ni2+, Ca2+, and Co2+are ineffective at stimulating activity. Monovalent ions are, in general, more effective the greater the ionic radius (NH+4Cs>Rb>K>Na). In contrast to the activity ofBacillus subtilis, C. sporogenesRNase P RNA is significant more active in (NH4)2SO4than in NH4Cl.