Showing papers by "Andreas G. Ladurner published in 2012"
Fred Hutchinson Cancer Research Center1, Harvard University2, Curie Institute3, University of Victoria4, National University of Singapore5, University of Melbourne6, University of California, Berkeley7, Florida State University8, University of California, Davis9, Rockefeller University10, Pennsylvania State University11, French Institute of Health and Medical Research12, University of Göttingen13, University of A Coruña14, University of Rochester15, Center for Integrated Protein Science Munich16, University of California17, University of California, Los Angeles18, Max Planck Society19, Joseph Fourier University20, Ludwig Maximilian University of Munich21, National Institutes of Health22, Claude Bernard University Lyon 123, University of North Carolina at Chapel Hill24, University of Pennsylvania25, Witten/Herdecke University26, University of Virginia27, University of Bergen28, University of Strasbourg29, Australian National University30, University of Birmingham31, University of Missouri–Kansas City32
TL;DR: A unified nomenclature for variants of all five classes of histones is proposed that uses consistent but flexible naming conventions to produce names that are informative and readily searchable and incorporates phylogenetic relationships, which are strong predictors of structure and function.
Abstract: Histone variants are non-allelic protein isoforms that play key roles in diversifying chromatin structure. The known number of such variants has greatly increased in recent years, but the lack of naming conventions for them has led to a variety of naming styles, multiple synonyms and misleading homographs that obscure variant relationships and complicate database searches. We propose here a unified nomenclature for variants of all five classes of histones that uses consistent but flexible naming conventions to produce names that are informative and readily searchable. The nomenclature builds on historical usage and incorporates phylogenetic relationships, which are strong predictors of structure and function. A key feature is the consistent use of punctuation to represent phylogenetic divergence, making explicit the relationships among variant subtypes that have previously been implicit or unclear. We recommend that by default new histone variants be named with organism-specific paralog-number suffixes that lack phylogenetic implication, while letter suffixes be reserved for structurally distinct clades of variants. For clarity and searchability, we encourage the use of descriptors that are separate from the phylogeny-based variant name to indicate developmental and other properties of variants that may be independent of structure.
301 citations
TL;DR: The crystal structure of the human PARP1-DBD bound to a DNA break is determined and reveals a dimeric assembly whereby ZnF1 andZnF2 domains from separatePARP1 molecules form a strand-break recognition module that helps activate PARP 1 by facilitating its dimerization and consequent trans-automodification.
Abstract: Poly(ADP-ribose) polymerase 1 (PARP1) is a primary DNA damage sensor whose (ADP-ribose) polymerase activity is acutely regulated by interaction with DNA breaks. Upon activation at sites of DNA damage, PARP1 modifies itself and other proteins by covalent addition of long, branched polymers of ADP-ribose, which in turn recruit downstream DNA repair and chromatin remodeling factors. PARP1 recognizes DNA damage through its N-terminal DNA-binding domain (DBD), which consists of a tandem repeat of an unusual zinc-finger (ZnF) domain. We have determined the crystal structure of the human PARP1-DBD bound to a DNA break. Along with functional analysis of PARP1 recruitment to sites of DNA damage in vivo, the structure reveals a dimeric assembly whereby ZnF1 and ZnF2 domains from separate PARP1 molecules form a strand-break recognition module that helps activate PARP1 by facilitating its dimerization and consequent trans-automodification.
213 citations
TL;DR: A number of exciting recent breakthroughs in understanding of the structural and mechanistic aspects of how PARP1 recognizes DNA, how PARPs are regulated, how ADP-ribose modifications are set onto specific targets and how the cellular machinery recognizes this elusive post-translational modification are summarized.
34 citations