Navigating the ribosome's metastable energy landscape. Review uri icon

Overview

MeSH

  • Binding Sites
  • Models, Molecular
  • Nucleic Acid Conformation
  • Thermodynamics

MeSH Major

  • Protein Biosynthesis
  • RNA, Messenger
  • RNA, Transfer
  • Ribosomes

abstract

  • The molecular mechanisms by which tRNA molecules enter and transit the ribosome during mRNA translation remains elusive. However, recent genetic, biochemical and structural studies offer important new findings into the ordered sequence of events underpinning the translocation process that help place the molecular mechanism within reach. In particular, new structural and kinetic insights have been obtained regarding tRNA movements through 'hybrid state' configurations. These dynamic views reveal that the macromolecular ribosome particle, like many smaller proteins, has an intrinsic capacity to reversibly sample an ensemble of similarly stable native states. Such perspectives suggest that substrates, factors and environmental cues contribute to translation regulation by helping the dynamic system navigate through a highly complex and metastable energy landscape.

publication date

  • August 2009

has subject area

  • Binding Sites
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Biosynthesis
  • RNA, Messenger
  • RNA, Transfer
  • Ribosomes
  • Thermodynamics

Research

keywords

  • Journal Article
  • Review

Identity

Language

  • eng

PubMed Central ID

  • PMC2914510

Digital Object Identifier (DOI)

  • 10.1016/j.tibs.2009.04.004

PubMed ID

  • 19647434

Additional Document Info

start page

  • 390

end page

  • 400

volume

  • 34

number

  • 8