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Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme.
Loria A, Niranjanakumari S, Fierke CA, Pan T. Loria A, et al. Among authors: niranjanakumari s. Biochemistry. 1998 Nov 3;37(44):15466-73. doi: 10.1021/bi9816507. Biochemistry. 1998. PMID: 9799509
Rather, the holoenzyme significantly affects the binding affinity of an RNA substrate through additional interactions with the 5' leader [Kurz, C. A., Niranjanakumari, S., and Fierke, C. A. (1998) Biochemistry 37, 2393] and through altered recognition of the substra …
Rather, the holoenzyme significantly affects the binding affinity of an RNA substrate through additional interactions with the 5' leader [Ku …
The protein component of Bacillus subtilis ribonuclease P increases catalytic efficiency by enhancing interactions with the 5' leader sequence of pre-tRNAAsp.
Crary SM, Niranjanakumari S, Fierke CA. Crary SM, et al. Among authors: niranjanakumari s. Biochemistry. 1998 Jun 30;37(26):9409-16. doi: 10.1021/bi980613c. Biochemistry. 1998. PMID: 9649323
To investigate the role of the protein component in enhancing the affinity of Bacillus subtilis RNase P for substrate (Kurz, J. C., Niranjanakumari, S., Fierke, C. A. (1998) Biochemistry 37, 2393), the kinetics and thermodynamics of binding and cleavage were analyze …
To investigate the role of the protein component in enhancing the affinity of Bacillus subtilis RNase P for substrate (Kurz, J. C., Niran …
22 results