PMID- 9539146
OWN - NLM
STAT- MEDLINE
DCOM- 19980427
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 424
IP  - 3
DP  - 1998 Mar 13
TI  - Determination of the human c-Abl consensus DNA binding site.
PG  - 177-82
AB  - c-Abl tyrosine kinase, an essential protein of the cell cycle signalling 
      pathways, is implicated in the regulation of RNA polymerase II activity, 
      apoptosis and DNA repair. Its DNA binding activity is important for its 
      biological functions. However, the molecular basis of c-Abl interaction with DNA 
      remains largely unclear. We delimited the human c-Abl DNA binding domain and 
      identified its preferred binding site, 5'-A(A/C)AACAA(A/C). The central AAC motif 
      is highly conserved and constitutes the major core element in the binding sites. 
      EMSAs and footprinting experiments were performed to explore how the c-Abl fusion 
      protein recognizes specific sequences in DNA.
FAU - David-Cordonnier, M H
AU  - David-Cordonnier MH
AD  - INSERM U 124 Onco-hematologie moleculaire, Institut de Recherches sur le Cancer 
      de Lille, France.
FAU - Hamdane, M
AU  - Hamdane M
FAU - Bailly, C
AU  - Bailly C
FAU - D'Halluin, J C
AU  - D'Halluin JC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Recombinant Fusion Proteins)
RN  - 9007-49-2 (DNA)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins c-abl)
RN  - EC 3.1.21.1 (Deoxyribonuclease I)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Binding Sites
MH  - Conserved Sequence
MH  - DNA/*metabolism
MH  - DNA Footprinting
MH  - Deoxyribonuclease I/metabolism
MH  - Electrophoresis/methods
MH  - Humans
MH  - Molecular Sequence Data
MH  - Protein Structure, Secondary
MH  - Proto-Oncogene Proteins c-abl/chemistry/genetics/*metabolism
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Deletion
MH  - Software
MH  - Substrate Specificity
EDAT- 1998/04/16 00:00
MHDA- 1998/04/16 00:01
CRDT- 1998/04/16 00:00
PHST- 1998/04/16 00:00 [pubmed]
PHST- 1998/04/16 00:01 [medline]
PHST- 1998/04/16 00:00 [entrez]
AID - S0014-5793(98)00169-0 [pii]
AID - 10.1016/s0014-5793(98)00169-0 [doi]
PST - ppublish
SO  - FEBS Lett. 1998 Mar 13;424(3):177-82. doi: 10.1016/s0014-5793(98)00169-0.