May, 2011
Volume 36, Issue 5

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Volume 36, Issue 5

Endogenous mechanisms and exogenous agents generate DNA single- and double-strand breaks that are a continual threat to the genome. Prompt and accurate repair is crucial to prevent genomic instability that precipitates cytotoxicity or neoplastic transformation. However, strand breaks frequently possess abnormal 5'-hydroxyl and 3'-phosphate ends that preclude the final enzymatic repair steps of nucleotide replacement by DNA polymerases and strand re-ligation by DNA ligases. Polynucleotide kinase/phosphatase (PNKP) contains dual 5'-DNA kinase/3'-DNA phosphatase activities and integrates both into single- and double-strand break repair mechanisms to re-engineer termini critical for restoring genomic continuity. Mutations to PNKP have recently been linked to a multi-symptom neurodevelopmental disorder. Clinically, PNKP function is a target for disruption in therapeutic chemo and radiosensitizing applications. On pages 262–271, Michael Weinfeld and colleagues discuss the structure and function of PNKP and how the enzyme is key for sustaining the edifice of DNA strand break repair. Cover design by R. Daniel Aceytuno.

Editorial Team

  • Editor
    Sara Cullinan
  • Acting Editor
    Gail Teitzel
  • Consulting Editor
    Rebecca Alvania
  • Executive Editor, Molecular Biology
    Feng Chen
  • Journal Manager
    Hanna van de Watering
  • Journal Administrator
    Mirjam Rietveld

Advisory
Editorial Board

  • Jan Witkowski
    Mariann Bienz
    Shamshad Cockcroft
    Jack Dixon
    Judith Frydman
    Toby Gibson
    Carl-Henrik Heldin
    Matthias Hentze
    Roger Kornberg
    Angus Lamond
    Titia de Lange
    Gregory Petsko
    Thomas Pollard
    Charles Sanders
    Paul Schimmel
    Peter H. von Hippel

Presubmission Inquiries

  • Articles are usually invited by the Editor; however, if you are interested in suggesting an article to the Editor for consideration please click here to submit a one to two page summary with a list of key references via the TiBS online presubmission inquiry form.

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Featured Article

DHHC palmitoyl transferases: substrate interactions and (patho)physiology
Jennifer Greaves, and Luke H. Chamberlain
10.1016/j.tibs.2011.01.003
Abstract | |

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In the May Issue

DHHC palmitoyl transferases: substrate interactions and (patho)physiology

Palmitoylation can spatiotemporally regulate proteins through diverse mechanisms. In this Review, Jennifer Greaves and Luke H. Chamberlain discuss the DHHC proteins, the family of enzymes that directs intracellular palmitoylation reactions, including recent findings that point to a role for these proteins in human health and disease .
*FREE DOWNLOAD*


Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair

Prompt and accurate DNA repair is essential for preventing genomic instability; however, strand breaks frequently possess abnormal ends that necessitate processing before the repair process can begin. PNKP, a dual 5'-DNA kinase/3'-DNA phosphatase, is able to perform such processing, thereby ensuring that repair can proceed as needed. In this review, Michael Weinfeld and colleagues discuss how PNPK structure contributes to its role in DNA repair and highlight how this information might be used in a clinical setting.


Also in this issue:

APOBEC3G: a double agent in defense

Mitochondrial protein quality control during biogenesis and aging

Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation

Molecular recognition and catalysis in translation termination complexes


Featured Topic: The RNA World

Although we often think of DNA as being the critical determinant of life on Earth, many investigators now believe that our origins lie in a so-called ‘RNA World’. How might this single-stranded molecule—which is often considered as a biological middle-man—have catalyzed life? This month, we feature a collection of articles that highlights the many ways in which RNA can catalyze complex chemical reactions and encode key genetic information.


The ribosome goes Nobel
Marina V. Rodnina and Wolfgang Wintermeyer

T2 Family ribonucleases: ancient enzymes with diverse roles
Natalie Luhtala and Roy Parker

The ribozyme core of group II introns: a structure in want of partners
François Michel, Maria Costa, and Eric Westhof

RNA helicases at work: binding and rearranging
Eckhard Jankowsky

Deconstructing ribosome construction
Keith Connolly and Gloria Culver

CRISPR-based adaptive and heritable immunity in prokaryotes
John van der Oost, Matthijs M. Jore, Edze R. Westra, Magnus Lundgren, and Stan J.J. Brouns

ADAR editing in double-stranded UTRs and other noncoding RNA sequences
Heather A. Hundley and Brenda L. Bass


Online publication ahead of print

TiBS publishes papers online ahead of the print issue. Here are some of the latest:

Gabius et al. From lectin structure to functional glycomics: principles of the sugar code Ute Woehlbier and Claudio Hetz Modulating stress responses by the UPRosome: A matter of life and death
Sanchez and Zhou The PHD finger: a versatile epigenome reader Bowzard et al. PAMPer and tRIGer: ligand-induced activation of RIG-I
Fändrich et al. Recent progress in understanding Alzheimer's β-amyloid structures Greenspan Attributing functions to genes and gene products

Most Read Articles RSS Icon Article Feed

These are the five most downloaded papers for the 30 days preceding May 22, 2011. See full list of most read articles

Regulation of intermediary metabolism by protein acetylation
Kun-Liang Guan, Yue Xiong
10.1016/j.tibs.2010.09.003
Summary | |
Mitochondrial protein quality control during biogenesis and aging
Brooke M. Baker, Cole M. Haynes
10.1016/j.tibs.2011.01.004
Summary | |
The tail of integrin activation
Nicholas J. Anthis, Iain D. Campbell
10.1016/j.tibs.2010.11.002
Summary | |
DHHC palmitoyl transferases: substrate interactions and (patho)physiology
Jennifer Greaves, Luke H. Chamberlain
10.1016/j.tibs.2011.01.003
Summary | |
Nuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation
Shigeaki Kato, Atsushi Yokoyama, Ryoji Fujiki
10.1016/j.tibs.2011.01.001
Summary | |