Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives.

Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Research Abstract Details 

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Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Abstract Text:

Steven A Kawamoto,Christopher G Sudhahar,Cynthia L Hatfield,Jing Sun,Edward J Behrman,Venkat Gopalan,

Ribonuclease P (RNase P) is a Mg2+-dependent endoribonuclease responsible for the 5'-maturation of transfer RNAs. It is a ribonucleoprotein complex containing an essential RNA and a varying number of protein subunits depending on the source: at least one, four and nine in Bacteria, Archaea and Eukarya, respectively. Since bacterial RNase P is required for viability and differs in structure/subunit composition from its eukaryal counterpart, it is a potential antibacterial target. To elucidate the basis for our previous finding that the hexa-arginine derivative of neomycin B is 500-fold more potent than neomycin B in inhibiting bacterial RNase P, we synthesized hexa-guanidinium and -lysyl conjugates of neomycin B and compared their inhibitory potential. Our studies indicate that side-chain length, flexibility and composition cumulatively account for the inhibitory potency of the aminoglycoside-arginine conjugates (AACs). We also demonstrate that AACs interfere with RNase P function by displacing Mg2+ ions. Moreover, our finding that an AAC can discriminate between a bacterial and archaeal (an experimental surrogate for eukaryal) RNase P holoenzyme lends promise to the design of aminoglycoside conjugates as selective inhibitors of bacterial RNase P, especially once the structural differences in RNase P from the three domains of life have been established.

Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Publishing Authors By Initials

SA Kawamoto,CG Sudhahar,CL Hatfield,J Sun,EJ Behrman,V Gopalan,

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Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Nucleic acids research

VOLUME: 36

Page Numbers: 697-704

Journal Abbreviation: Nucleic Acids Res.

ISSN: 1362-4962

DAY: 15

MONTH: 12

YEAR: 2007

Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Information

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LANGUAGE: eng

NlmUniqueID: 411011

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Grant and Affiliation Information for Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives.

AFFILIATION: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA.

Country: England

AGENCY: United States NIGMS

GRANT: R01 GM067807

ACRONYM: GM

MEDLINETA: Nucleic Acids Res

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