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Volume 272, Number 24, Issue of June 13, 1997 pp. 15339-15345
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Deletion Analysis of Q Replicase
PARTICIPATION OF THE CARBOXYL-TERMINAL REGION OF THE -SUBUNIT PROTEIN IN TEMPLATE RECOGNITION

(Received for publication, October 23, 1996, and in revised form, March 19, 1997)

From the Department of Biosciences, Teikyo University, 1-1 Toyosatodai, Utsunomiya-shi, Tochigi 320, Japan

We have analyzed one of the functional domains of Q replicase, an RNA-dependent RNA polymerase of RNA coliphage Q. Deletion mapping analysis of the carboxyl-terminal region of the -subunit protein revealed that the terminal 18 amino acid residues (positions 571-588) are dispensable for the replicase reaction. Subsequent deletions up to the Ala-565 residue reduced the RNA polymerizing activity of the replicase in vivo but increased it in vitro. The mutant replicases with enhanced in vitro RNA polymerizing activity were found to have relaxed template specificity for ribosomal RNAs and cellular RNAs as well as Q RNA. Deletions beyond the Ile-564 residue abolished both the RNA polymerizing activity and the binding ability to midivariant (MDV)-poly(+) RNA, a derivative of a natural template for Q replicase, MDV-1 RNA. These results suggest that the carboxyl-terminal part of the -subunit participates in RNA recognition of Q replicase.

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