scholarly journals In vitro analysis of processing at the 3'-end of precursors of M1 RNA, the catalytic subunit of Escherichia coli RNase P: Multiple pathways and steps for the processing

1999 ◽  
Vol 27 (3) ◽  
pp. 895-902 ◽  
Author(s):  
S. Kim ◽  
S. Sim ◽  
Y. Lee
1986 ◽  
Vol 6 (2) ◽  
pp. 525-529
Author(s):  
O Orellana ◽  
L Cooley ◽  
D Söll

In eucaryotes the 5'-terminal guanylate moiety of mature tRNAHis is added posttranscriptionally. To determine whether the same mechanism occurs in procaryotes, we processed in vitro-derived Escherichia coli tRNAHis precursors to mature tRNA, either in E. coli extracts or by using pure M1-RNA, the catalytic component of RNase P. The results show that the extra guanylate at the 5' end of mature E. coli tRNAHis is encoded in the gene and is found in tRNA as the result of an unusual cleavage by RNase P.


2011 ◽  
Vol 186 (4S) ◽  
pp. 1678-1683 ◽  
Author(s):  
Douglas W. Storm ◽  
Stephen A. Koff ◽  
Dennis J. Horvath ◽  
Birong Li ◽  
Sheryl S. Justice

1986 ◽  
Vol 6 (2) ◽  
pp. 525-529 ◽  
Author(s):  
O Orellana ◽  
L Cooley ◽  
D Söll

In eucaryotes the 5'-terminal guanylate moiety of mature tRNAHis is added posttranscriptionally. To determine whether the same mechanism occurs in procaryotes, we processed in vitro-derived Escherichia coli tRNAHis precursors to mature tRNA, either in E. coli extracts or by using pure M1-RNA, the catalytic component of RNase P. The results show that the extra guanylate at the 5' end of mature E. coli tRNAHis is encoded in the gene and is found in tRNA as the result of an unusual cleavage by RNase P.


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