PMID- 26556350
OWN - NLM
STAT- MEDLINE
DCOM- 20160819
LR  - 20181113
IS  - 1422-0067 (Electronic)
IS  - 1422-0067 (Linking)
VI  - 16
IP  - 11
DP  - 2015 Nov 5
TI  - Protein Recognition in Drug-Induced DNA Alkylation: When the Moonlight Protein 
      GAPDH Meets S23906-1/DNA Minor Groove Adducts.
PG  - 26555-81
LID - 10.3390/ijms161125971 [doi]
AB  - DNA alkylating drugs have been used in clinics for more than seventy years. The 
      diversity of their mechanism of action (major/minor groove; mono-/bis-alkylation; 
      intra-/inter-strand crosslinks; DNA stabilization/destabilization, etc.) has 
      undoubtedly major consequences on the cellular response to treatment. The aim of 
      this review is to highlight the variety of established protein recognition of DNA 
      adducts to then particularly focus on glyceraldehyde-3-phosphate dehydrogenase 
      (GAPDH) function in DNA adduct interaction with illustration using original 
      experiments performed with S23906-1/DNA adduct. The introduction of this review 
      is a state of the art of protein/DNA adducts recognition, depending on the major 
      or minor groove orientation of the DNA bonding as well as on the molecular 
      consequences in terms of double-stranded DNA maintenance. It reviews the 
      implication of proteins from both DNA repair, transcription, replication and 
      chromatin maintenance in selective DNA adduct recognition. The main section of 
      the manuscript is focusing on the implication of the moonlighting protein GAPDH 
      in DNA adduct recognition with the model of the peculiar DNA minor groove 
      alkylating and destabilizing drug S23906-1. The mechanism of action of S23906-1 
      alkylating drug and the large variety of GAPDH cellular functions are presented 
      prior to focus on GAPDH direct binding to S23906-1 adducts.
FAU - Savreux-Lenglet, Gaelle
AU  - Savreux-Lenglet G
AD  - UMR-S1172-Jean-Pierre Aubert Research Centre (JPARC), INSERM, University of 
      Lille, Lille Hospital, Institut pour la Recherche sur le Cancer de Lille, Place 
      de Verdun F-59045 Lille cedex, France. gaelle.lenglet@u-picardie.fr.
FAU - Depauw, Sabine
AU  - Depauw S
AD  - UMR-S1172-Jean-Pierre Aubert Research Centre (JPARC), INSERM, University of 
      Lille, Lille Hospital, Institut pour la Recherche sur le Cancer de Lille, Place 
      de Verdun F-59045 Lille cedex, France. sabine.depauw@inserm.fr.
FAU - David-Cordonnier, Marie-Helene
AU  - David-Cordonnier MH
AD  - UMR-S1172-Jean-Pierre Aubert Research Centre (JPARC), INSERM, University of 
      Lille, Lille Hospital, Institut pour la Recherche sur le Cancer de Lille, Place 
      de Verdun F-59045 Lille cedex, France. marie-helene.david@inserm.fr.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20151105
PL  - Switzerland
TA  - Int J Mol Sci
JT  - International journal of molecular sciences
JID - 101092791
RN  - 0 (Alkylating Agents)
RN  - 0 (DNA Adducts)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Transcription Factors)
RN  - 9007-49-2 (DNA)
RN  - EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating))
SB  - IM
MH  - Alkylating Agents/*pharmacology
MH  - Alkylation
MH  - Cell Nucleus
MH  - Cytoplasm
MH  - DNA/*chemistry/*metabolism
MH  - DNA Adducts/*metabolism
MH  - DNA Damage
MH  - DNA Replication
MH  - DNA-Binding Proteins/*metabolism
MH  - Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)/metabolism
MH  - Nucleic Acid Conformation
MH  - Protein Binding
MH  - Transcription Factors/metabolism
PMC - PMC4661830
OTO - NOTNLM
OT  - DNA alkylation
OT  - DNA repair
OT  - Glyceraldehyde-3-phosphate dehydrogenase
OT  - S23906-1
OT  - protein/DNA binding
EDAT- 2015/11/12 06:00
MHDA- 2016/08/20 06:00
PMCR- 2015/11/01
CRDT- 2015/11/12 06:00
PHST- 2015/08/05 00:00 [received]
PHST- 2015/10/25 00:00 [revised]
PHST- 2015/10/27 00:00 [accepted]
PHST- 2015/11/12 06:00 [entrez]
PHST- 2015/11/12 06:00 [pubmed]
PHST- 2016/08/20 06:00 [medline]
PHST- 2015/11/01 00:00 [pmc-release]
AID - ijms161125971 [pii]
AID - ijms-16-25971 [pii]
AID - 10.3390/ijms161125971 [doi]
PST - epublish
SO  - Int J Mol Sci. 2015 Nov 5;16(11):26555-81. doi: 10.3390/ijms161125971.