Can I read Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex on EtoBox?

Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex by Wen-Yi Chen; Dileep K. Pulukkunat; I-Ming Cho; Hsin-Yue Tsai; Venkat Gopalan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex about?

RNase P catalyzes the Mg^2^^+^-dependent 5′-maturation of precursor tRNAs. Biochemical studies on the bacterial holoenzyme, composed of one catalytic RNase P RNA (RPR) and one RNase P protein (RPP), have helped understand the pleiotropic roles (including substrate/Mg^2+^ binding) by which a protein could facilitate RNA catalysis. As a model for uncovering the functional coordination among multiple proteins that aid an RNA catalyst, we use archaeal RNase P, which comprises one catalytic RPR and at least four RPPs. Exploiting our previous finding that these archaeal RPPs function as two binary RPP complexes (POP5•RPP30 and RPP21•RPP29), we prepared recombinant RPP pairs from three archaea and established interchangeability of subunits through homologous/heterologous assemblies. Our finding that archaeal POP5•RPP30 reconstituted with bacterial and organellar RPRs suggests functional overlap of this binary complex with the bacterial RPP and highlights their shared recognition of a phylogenetically-conserved RPR catalytic core, whose minimal attributes we further defined through deletion mutagenesis. Moreover, single-turnover kinetic studies revealed that while POP5•RPP30 is solely resp

Who reads Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex?

Author

Wen-Yi Chen; Dileep K. Pulukkunat; I-Ming Cho; Hsin-Yue Tsai; Venkat Gopalan

Publisher

Oxford University Press

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)