PMID- 9765261
OWN - NLM
STAT- MEDLINE
DCOM- 19981106
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 42
DP  - 1998 Oct 16
TI  - An extended alpha-helix and specific amino acid residues opposite the DNA-binding 
      surface of the cAMP response element binding protein basic domain are important 
      for human T cell lymphotropic retrovirus type I Tax binding.
PG  - 27339-46
AB  - The human T cell lymphotropic retrovirus type I (HTLV-I) trans-activator, Tax, 
      interacts specifically with the basic-domain/leucine-zipper (bZip) protein, cAMP 
      response element binding protein (CREB), bound to the viral Tax-responsive 
      element consisting of three imperfect 21-base pair repeats, each with a cAMP 
      response element core flanked by G/C-rich sequences. Here, the minimal CREB-bZip 
      necessary for Tax binding is shown to be composed of amino acid residues 280-341. 
      The Tax-CREB interaction involves an uninterrupted and extended alpha-helix in 
      CREB that spans most of its basic domain to include amino acid residues localized 
      to the NH2 terminus of the DNA binding region. Mutational analyses indicate that 
      three residues, Arg284, Met291, and Glu299 unique to this region of the 
      CREB/activating transcription factor-1 subfamily of bZip proteins, constitute the 
      contact surface for Tax. Amino acid substitutions in these positions had little 
      impact on CREB-bZip binding to DNA but abrogated its binding to Tax. Each of the 
      contact residues for Tax are spaced approximately two helical turns apart on the 
      side of the bZip helix directly opposite to that of the invariant DNA-binding 
      residues. Molecular modeling reveals the Tax-contact residues to be near the 
      minor groove of the G/C-rich DNA in the 21-base pair repeat. They most likely 
      position Tax for minor groove contact with the G/C-rich sequences.
FAU - Tang, Y
AU  - Tang Y
AD  - Department of Microbiology and Immunology, Uniformed Services University, 
      Bethesda, Maryland 20814, USA.
FAU - Tie, F
AU  - Tie F
FAU - Boros, I
AU  - Boros I
FAU - Harrod, R
AU  - Harrod R
FAU - Glover, M
AU  - Glover M
FAU - Giam, C Z
AU  - Giam CZ
LA  - eng
GR  - R0 CA/GM 75688/CA/NCI NIH HHS/United States
GR  - R01 CA48709/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cyclic AMP Response Element-Binding Protein)
RN  - 0 (DNA, Viral)
RN  - 0 (Gene Products, tax)
RN  - 0 (Peptide Fragments)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Computer Simulation
MH  - Crystallography, X-Ray
MH  - Cyclic AMP Response Element-Binding Protein/*chemistry/genetics/*metabolism
MH  - DNA, Viral/*metabolism
MH  - Gene Expression Regulation, Viral
MH  - Gene Products, tax/*metabolism
MH  - Human T-lymphotropic virus 1/*genetics
MH  - Leucine Zippers
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry/genetics/metabolism
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Regulatory Sequences, Nucleic Acid
EDAT- 1998/10/09 00:00
MHDA- 1998/10/09 00:01
CRDT- 1998/10/09 00:00
PHST- 1998/10/09 00:00 [pubmed]
PHST- 1998/10/09 00:01 [medline]
PHST- 1998/10/09 00:00 [entrez]
AID - S0021-9258(19)59678-8 [pii]
AID - 10.1074/jbc.273.42.27339 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 Oct 16;273(42):27339-46. doi: 10.1074/jbc.273.42.27339.