Proteomics articles within Nature

Featured

  • Letter |

    Affinity tagging, mass spectroscopy and a tailor-made scoring system are used to identify 497 high-confidence interactions between human proteins and human immunodeficiency virus proteins.

    • Stefanie Jäger
    • , Peter Cimermancic
    •  & Nevan J. Krogan
  • Article |

    A meta-analysis of genome-wide association studies in more than 66,000 individuals identifies 68 new genomic loci that reliably associate with platelet count and volume, and reveals new gene functions.

    • Christian Gieger
    • , Aparna Radhakrishnan
    •  & Nicole Soranzo
  • News & Views |

    The protein Hsp90 is a target of promising anticancer drugs. An analysis of the components of Hsp90 complexes in tumours reveals a path that may lead to predictive assays of drug sensitivity in cancer patients.

    • John F. Darby
    •  & Paul Workman
  • News & Views |

    An innovative marriage of techniques, combining the principles of common protein pull-down assays with single-molecule fluorescence microscopy, opens up new ways of visualizing cellular protein complexes. See Article p.484

    • Philip Tinnefeld
  • Technology Feature |

    Developing techniques are helping researchers to build the protein interaction networks that underlie all cell functions.

    • Laura Bonetta
  • Article |

    Cysteine is the most intrinsically nucleophilic amino acid in proteins, but the absence of a consensus sequence that defines functional cysteines in proteins has hindered their discovery and characterization. Here, a proteomics method to quantitatively profile the intrinsic reactivity of cysteine residues directly in native biological systems is described. Hyper-reactive cysteines were identified in several proteins of uncharacterized function, including a residue conserved across eukaryotes that is shown to be required for yeast viability and involved in iron–sulphur protein biogenesis.

    • Eranthie Weerapana
    • , Chu Wang
    •  & Benjamin F. Cravatt
  • Article |

    The two hereditary breast cancer susceptibility genes, BRCA1 and BRCA2, have roles in responding to DNA damage. When they are mutated or absent, genomic instability, a contributory factor to cancer development, results. Studies of BRCA2 have been hampered by its large size, which makes purification of the full-length protein challenging. These authors report the first in vitro characterization of full-length BRCA2 and delineate the different ways by which BRCA2 facilitates RAD51-mediated homologous recombination.

    • Ryan B. Jensen
    • , Aura Carreira
    •  & Stephen C. Kowalczykowski
  • Article |

    Autophagy is a cellular process by which proteins and organelles are sequestered in autophagosomal vesicles and delivered to the lysosome for degradation. Here the authors present a proteomic analysis of the autophagy interaction network in human cells. Their results reveal a network of signalling modules and extensive connectivity among subnetworks. This global view of the mammalian autophagy pathway will be an important resource for future mechanistic understanding of this pathway.

    • Christian Behrends
    • , Mathew E. Sowa
    •  & J. Wade Harper
  • Letter |

    Nascent secretory or membrane proteins contain an amino-terminal signal peptide that mediates their targeting to the plasma membrane (in prokaryotes) or endoplasmic reticulum (in eukaryotes). This peptide is recognized by the signal recognition particle (SRP). A universally conserved component of the SRP is known as SRP54 (Ffh in bacteria). Here, the crystal structure of Sulfolobus solfataricus SRP54 fused to a signal peptide is presented, revealing how the signal peptide is recognized by SRP54.

    • Claudia Y. Janda
    • , Jade Li
    •  & Kiyoshi Nagai
  • News & Views |

    The production of intestinal cells in a worm embryo is regulated by a network of transcription factors. Studies of these networks in mutant worms provide evidence for stochastic effects in gene expression.

    • Adrian Streit
    •  & Ralf J. Sommer
  • Letter |

    Polycomb proteins have a key role in regulating the expression of genes essential for development, differentiation and maintenance of cell fates. Here, Polycomb repressive complex 2 (PRC2) is shown to form a complex with JARID2, a Jumonji domain protein. JARID2 is required for the binding of Polycomb proteins to target genes in embryonic stem cells as well as for the proper differentiation of ES cells.

    • Diego Pasini
    • , Paul A. C. Cloos
    •  & Kristian Helin