[Properties of antigenomic HDV ribozyme consisting of two RNA chains].
B : LS ribozyme, a trans-variant of naturally occurring HDV ribozyme, has been constructed. The ribozyme consists of a substrate-containing LS chain and an enzyme B chain and differs from previously constructed trans-ribozymes in the length and nucleotide sequence of its oligonucleotide chains (34 and 33 bp, respectively). The chains readily associate with each other at a room temperature while the LS cleavage reaction at this temperature is negligible slow, which allowed us to investigate the association of the intact chains. At the same time the self-cleavage rate constant for the trans-ribozyme B : LS at 50 degrees C is close to those for the previously studied permuted cis-ribozymes, especially LSB variant. In addition, the dependence on the reaction conditions (Mg2+ concentration, pH, temperature) of the trans-ribozyme was similar to that of cis-ribozyme. Similar to other trans-ribozymes, B : LS ribozyme demonstrates the ability for multiple use of the enzyme B-chain with an excess of the substrate LS chain. The kinetics model of self-cleavage reaction for B : LS is presented in http://www.cardio.ru/labgen/RZ_r.html. Taken together, our results show that the original trans-variant of HDV ribozyme can be used as a model for the investigation of self-cleavage process of HDV ribozymes.
Alekseenkova
V A
VA
Belianko
T I
TI
Lukin
M A
MA
Savichkina
L P
LP
Bibilashvili
R Sh
RSh
D001483:Base Sequence; D016679:Genome, Viral; D003698:Hepatitis Delta Virus / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000737:chemistry; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism*; D013696:Temperature
D016337:RNA, Catalytic; D008274:Magnesium