Abstract
The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. Previous biochemical data indicate that it binds to two stem-loops in RNase P RNA (PhopRNA). Thermodynamic analysis revealed that PhoRpp38 and PhopRNA interact with each other with an association constant (Ka) of 1.56×10(7) M(-1). It was further found that PhoRpp38 simultaneously binds two stem-loop structures in PhopRNA with approximately equal affinity. Crystals of PhoRpp38 in complex with the stem-loop were grown and diffracted to a resolution of 7.0 Å on a synchrotron X-ray source.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / metabolism
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Binding Sites
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Calorimetry
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Crystallography, X-Ray
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Electrophoretic Mobility Shift Assay
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Hot Temperature
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Inverted Repeat Sequences
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Kinetics
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Molecular Sequence Data
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Mutation
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Protein Binding
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Pyrococcus horikoshii / genetics
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Pyrococcus horikoshii / metabolism*
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RNA, Archaeal / chemistry*
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RNA, Archaeal / genetics
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RNA, Archaeal / metabolism
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Ribonuclease P / chemistry*
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Ribonuclease P / genetics
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Ribonuclease P / metabolism
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Thermodynamics
Substances
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Archaeal Proteins
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RNA, Archaeal
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Ribonuclease P