Wr. Hess et al., RNASE P RNA FROM PROCHLOROCOCCUS-MARINUS - CONTRIBUTION OF SUBSTRATE DOMAINS TO RECOGNITION BY A CYANOBACTERIAL RIBOZYME, FEBS letters, 431(2), 1998, pp. 138-142
The molecular organisation of the Prochlorococcus marinus rnpB gene an
d the catalytic activity of the encoded RNA were characterised. Kineti
c parameters for several pre-tRNA substrates were comparable to those
from other eubacterial RNase P RNAs, although unusually high cation co
ncentrations were required. The CCA-end of pre-tRNAs is essential for
efficient turnover despite the lack of the canonical binding motif in
P. marinus RNase P RNA. A trnR gene is located only 38 nt upstream the
rnpB 5' end on the complementary strand. This arrangement resembles t
hose in the plastids of Cyanophora and Porphyra but not in any other b
acterium. (C) 1998 Federation of European Biochemical Societies.