Comparative analysis of RNAses barnase and binase: method of hybrid genes
Kurbanov, F.T.; Shul'ga, A.A.; Ranjbar, B.; Makarov, A.A.; Kirpichnikov, M.P.
Molekuliarnaia Biologiia 31(6): 1057-1063
1997
ISSN/ISBN: 0026-8984 PMID: 9480419 Document Number: 482395
Hybrid Rnases comprising segments of barnase (Ba) and binase (Bi) from Bacillus amyloliauefaciens: (1-25)Ba/(26-110)Bi, (172)Ba/(73-110)Bi, (1-25)Ba/(26-72))Bi/(73-110)Ba, and (1-72)Bi/(73-110)Ba, were compared in their catalytic properties with GpC, GpU, poly(A) and poly(I) as substrates. The nature of the C-proximal part of the RNase molecules (amino acid residues 73-110) was shown to determine not only the catalytic properties of enzymes with low-molecular substrates, but also the heat stability at acidic pH. On poly(I), the activity of hybrids was significantly higher than that of binase, and was inversely correlated with heat stability of the protein at near-neutral pH.