Comparison of transfer RNA and ribosomal RNA intron splicing in the extreme thermophile and archaebacterium Desulfurococcus mobilis

1989 ◽  
Vol 35 (1) ◽  
pp. 210-214 ◽  
Author(s):  
Jørgen Kjems ◽  
Jonna Jensen ◽  
Tina Olesen ◽  
Roger A. Garrett

The structure of the exon–intron boundary was compared for an intron within 23S ribosomal RNA of Desulfurococcus mobilis and a newly discovered intron in tRNAMet from the same organism. The occurrence of a putative common structural feature suggests that intron excision occurs by the same mechanism. The possible recognition of this structural feature by the cleavage enzyme was investigated for the ribosomal RNA intron using RNA substrates exhibiting various exon and intron deletions. The results support the involvement of the structural features in the cleavage process. The evolutionary implications of these results are considered.Key words: archaebacteria, tRNA, ribosomal RNA, introns, intron evolution.

2011 ◽  
Vol 49 (3) ◽  
pp. 508-511 ◽  
Author(s):  
Woo-Seok Song ◽  
Minho Lee ◽  
Kangseok Lee

1991 ◽  
Vol 70 (6) ◽  
pp. 961-965 ◽  
Author(s):  
G.J. Sunday ◽  
M.J. Gillespie ◽  
S.T. Motley ◽  
J.J. Zambon

RNA ◽  
2011 ◽  
Vol 18 (2) ◽  
pp. 345-353 ◽  
Author(s):  
N. S. Gutgsell ◽  
C. Jain

1986 ◽  
Vol 6 (8) ◽  
pp. 759-766 ◽  
Author(s):  
Peter W. Goodenough ◽  
Peter J. Kilshaw ◽  
Fiona McEwan ◽  
A. Jane Owen

The proteinases from Carica papaya include papain, isoenzymes of chymopapain and two proteinases A and B distinguished by their unusually high pI. The identity of one of the most basic proteinases has been questioned. The present report describes the preparation and characterisation of two monoclonal antibodies that react specifically with papaya proteinases A and B respectively and a third that identifies a common structural feature found in papain and proteinase A.


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