Volume 10 Issue 6, June 2009

Volume 10 Issue 6

'Second wave' by Vicky Summersby, inspired by the Review on p410.

From The Editors

Research Highlights

Reviews

  • Review Article |

    ATP-dependent chromatin-remodelling complexes are well-known regulators of transcriptional processes. Interestingly, the INO80 and SWR1 complexes also participate in a range of pathways that are involved in genome maintenance, such as DNA repair, checkpoint regulation, DNA replication, chromosome segregation and telomere stabilization.

    • Ashby J Morrison
    •  & Xuetong Shen
  • Review Article |

    The ubiquitin–26S proteasome system is one of the most pervasive pathways of intracellular protein regulation in plants. It controls hormone signalling, chromatin structure and transcription, tailoring morphogenesis, responses to environmental challenges, self-recognition and the battle between pathogens and their plant hosts.

    • Richard D. Vierstra
  • Review Article |

    Ubiquitylation targets proteins for degradation or other cellular fates. The HECT enzymes are E3 ubiquitin ligases, which dictate the specificity of ubiquitylation. HECTs regulate trafficking of many receptors, channels, transporters and viral proteins. Their role in metazoans is becoming clearer from in vivo studies.

    • Daniela Rotin
    •  & Sharad Kumar
  • Review Article |

    Synthetic biology combines the investigative nature of biology with the constructive nature of engineering. A 'first wave' in the field has led to the creation of genetic devices and small modules that are constructed from these devices. Now, a 'second wave' is required to develop effective strategies for assembling devices and modules into intricate customizable larger scale systems.

    • Priscilla E. M. Purnick
    •  & Ron Weiss

Perspectives

    Opinions

  • Opinion |

    Guanine nucleotide-binding (G) proteins are regulated by GTPase-activating proteins and guanine nucleotide-exchange factors. Another class of G proteins is emerging that are regulated by homodimerization. The authors propose that juxtaposition of the G domains of two monomers across the GTP-binding sites activates the biological function of these proteins and the GTPase reaction.

    • Raphael Gasper
    • , Simon Meyer
    • , Katja Gotthardt
    • , Minhajuddin Sirajuddin
    •  & Alfred Wittinghofer