PMID- 12198117
OWN - NLM
STAT- MEDLINE
DCOM- 20030206
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 277
IP  - 45
DP  - 2002 Nov 8
TI  - Sex-specific gene regulation. The Doublesex DM motif is a bipartite DNA-binding 
      domain.
PG  - 43463-73
AB  - Sex-specific gene expression in Drosophila melanogaster is regulated in part by 
      the Doublesex (DSX) transcription factor. Male- and female-specific splicing 
      isoforms share a novel DNA-binding domain, designated the DM motif. This domain 
      is conserved among a newly recognized family of vertebrate transcription factors 
      involved in developmental patterning and sex determination. The DM motif consists 
      of an N-terminal zinc module and a disordered C-terminal tail, hypothesized to 
      fold on specific DNA binding as a recognition alpha-helix. Truncation of the tail 
      does not perturb the structure of the zinc module but impairs DNA binding and 
      DNA-dependent dimerization. Chemical protein synthesis and alanine scanning 
      mutagenesis are employed to test the contributions of 13 side chains to specific 
      DNA binding. Selected arginine or lysine residues in the zinc module were 
      substituted by norleucine, an isostere that maintains the aliphatic portion of 
      the side chain but lacks a positive charge. Arginine or glutamine residues in the 
      tail were substituted by alanine. Evidence is obtained that both the zinc module 
      and C-terminal tail contribute to a bipartite DNA-binding surface. Conserved 
      arginine and glutamine residues in the tail are required for high affinity DNA 
      recognition, consistent with its proposed role as a nascent recognition 
      alpha-helix.
FAU - Narendra, Uma
AU  - Narendra U
AD  - Department of Biochemistry, Case Western Reserve University School of Medicine, 
      Cleveland, Ohio 44106, USA.
FAU - Zhu, Lingyang
AU  - Zhu L
FAU - Li, Biaoru
AU  - Li B
FAU - Wilken, Jill
AU  - Wilken J
FAU - Weiss, Michael A
AU  - Weiss MA
LA  - eng
SI  - PDB/1LPV
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20020826
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (DSX protein, Drosophila)
RN  - 0 (Drosophila Proteins)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Caenorhabditis elegans/metabolism
MH  - Caenorhabditis elegans Proteins/metabolism
MH  - Conserved Sequence
MH  - DNA/metabolism
MH  - DNA-Binding Proteins/chemistry/*metabolism
MH  - Drosophila Proteins/chemistry/*metabolism
MH  - Drosophila melanogaster/*physiology
MH  - Female
MH  - *Gene Expression Regulation/physiology
MH  - Male
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Sex Characteristics
EDAT- 2002/08/29 10:00
MHDA- 2003/02/07 04:00
CRDT- 2002/08/29 10:00
PHST- 2002/08/29 10:00 [pubmed]
PHST- 2003/02/07 04:00 [medline]
PHST- 2002/08/29 10:00 [entrez]
AID - S0021-9258(19)71952-8 [pii]
AID - 10.1074/jbc.M204616200 [doi]
PST - ppublish
SO  - J Biol Chem. 2002 Nov 8;277(45):43463-73. doi: 10.1074/jbc.M204616200. Epub 2002 
      Aug 26.