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Structures of ribonucleoprotein particle modification enzymes

Published online by Cambridge University Press:  26 November 2010

Bo Liang  and
Hong Li
Bo Liang
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32312, USA
Hong Li*
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32312, USA Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32312, USA
*
*Author for correspondence: H. Li, Institute of Molecular Biophysics, Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32312, USA. Tel.: (850) 644–6785; Email: [email protected]
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Abstract

Small nucleolar and Cajal body ribonucleoprotein particles (RNPs) are required for the maturation of ribosomes and spliceosomes. They consist of small nucleolar RNA or Cajal body RNA combined with partner proteins and represent the most complex RNA modification enzymes. Recent advances in structure and function studies have revealed detailed information regarding ribonucleoprotein assembly and substrate binding. These enzymes form intertwined RNA–protein assemblies that facilitate reversible binding of the large ribosomal RNA or small nuclear RNA. These revelations explain the specificity among the components in enzyme assembly and substrate modification. The multiple conformations of individual components and those of complete RNPs suggest a dynamic assembly process and justify the requirement of many assembly factors in vivo.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 44 , Issue 1 , February 2011 , pp. 95 - 122
Copyright
Copyright © Cambridge University Press 2010

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