Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity.

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Research Abstract Details 

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Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Abstract Text:

Lei Sun,Michael E Harris,

The RNA subunit (P RNA) of the bacterial RNase P ribonucleoprotein is a ribozyme that catalyzes the Mg-dependent hydrolysis of pre-tRNA, but it requires an essential protein cofactor (P protein) in vivo that enhances substrate binding affinities and catalytic rates in a substrate dependent manner. Previous studies of Bacillus subtilis RNase P, containing a Type B RNA subunit, showed that its cognate protein subunit increases the affinity of metal ions important for catalysis, but the functional role of these ions is unknown. Here, we demonstrate that the Mg2+ dependence of the catalytic step for Escherichia coli RNase P, which contains a more common Type A RNA subunit, is also modulated by its cognate protein subunit (C5), indicating that this property is fundamental to P protein. To monitor specifically the binding of active site metal ions, we analyzed quantitatively the rescue by Cd2+ of an inhibitory Rp phosphorothioate modification at the pre-tRNA cleavage site. The results show that binding of C5 protein increases the apparent affinity of the rescuing Cd2+, providing evidence that C5 protein enhances metal ion affinity in the active site, and thus is likely to contribute significantly to rate enhancement at physiological metal ion concentrations.

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Publishing Authors By Initials

L Sun,ME Harris,

For similar ribonuclease p research abstracts see: ribonuclease p research

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MEDLINE DATE:

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: RNA (New York, N.Y.)

VOLUME: 13

Page Numbers: 1505-15

Journal Abbreviation: RNA

ISSN: 1355-8382

DAY: 25

MONTH: 07

YEAR: 2007

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9509184

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Keywords Mesh Terms:

KEYWORDS: Ribonuclease P

MESH TERMS: metabolism

Chemical & Substance for Abstract: Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. Information

Substance Name: ribonuclease P, E coli

Registry Number: EC 3.1.26.5

Grant and Affiliation Information for Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity.

AFFILIATION: Center for RNA Molecular Biology, Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM56742

ACRONYM: GM

MEDLINETA: RNA

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