PMID- 10523646
OWN - NLM
STAT- MEDLINE
DCOM- 19991124
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 11
DP  - 1999 Nov
TI  - PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins.
PG  - 7577-88
AB  - HOX, PBX, and MEIS transcription factors bind DNA through a homeodomain. PBX
      proteins bind DNA cooperatively as heterodimers with MEIS family members and also
      with HOX proteins from paralog groups 1 to 10. MEIS proteins cooperatively bind
      DNA with ABD-B class HOX proteins of groups 9 and 10. Here, we examine aspects of
      dimeric and higher-order interactions between these three homeodomain classes.
      The most significant results can be summarized as follows. (i) Most of PBX N
      terminal to the homeodomain is required for efficient cooperative binding with
      HOXD4 and HOXD9. (ii) MEIS and PBX proteins form higher-order complexes on a
      heterodimeric binding site. (iii) Although MEIS does not cooperatively bind DNA
      with ANTP class HOX proteins, it does form a trimer as a non-DNA-binding partner 
      with DNA-bound PBX-HOXD4. (iv) The N terminus of HOXD4 negatively regulates
      trimer formation. (v) MEIS forms a similar trimer with DNA-bound PBX-HOXD9. (vi) 
      A related trimer (where MEIS is a non-DNA-binding partner) is formed on a
      transcriptional promoter within the cell. (vii) We observe an additional trimer
      class involving non-DNA-bound PBX and DNA-bound MEIS-HOXD9 or MEIS-HOXD10
      heterodimers that is enhanced by mutation of the PBX homeodomain. (viii) In this 
      latter trimer, PBX is likely to contact both MEIS and HOXD9/D10. (ix) The
      stability of DNA binding by all trimers is enhanced relative to the heterodimers.
      These findings suggest novel functions for PBX and MEIS in modulating the
      function of DNA-bound MEIS-HOX and PBX-HOX heterodimers, respectively.
FAU - Shanmugam, K
AU  - Shanmugam K
AD  - McGill Cancer Centre, McGill University, Montreal, Quebec, Canada H3G 1Y6.
FAU - Green, N C
AU  - Green NC
FAU - Rambaldi, I
AU  - Rambaldi I
FAU - Saragovi, H U
AU  - Saragovi HU
FAU - Featherstone, M S
AU  - Featherstone MS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Antennapedia Homeodomain Protein)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Homeodomain Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Myeloid Ecotropic Viral Integration Site 1 Protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Pre-B-Cell Leukemia Transcription Factor 1)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (pbx1 protein, human)
SB  - IM
MH  - Antennapedia Homeodomain Protein
MH  - Binding Sites
MH  - DNA-Binding Proteins/metabolism
MH  - Dimerization
MH  - Homeodomain Proteins/classification/*metabolism
MH  - Macromolecular Substances
MH  - Models, Genetic
MH  - Multigene Family
MH  - Myeloid Ecotropic Viral Integration Site 1 Protein
MH  - Neoplasm Proteins/metabolism
MH  - *Nuclear Proteins
MH  - Pre-B-Cell Leukemia Transcription Factor 1
MH  - Protein Binding
MH  - Protein Structure, Quaternary
MH  - Proto-Oncogene Proteins/metabolism
MH  - Transcription Factors/classification/*metabolism
PMC - PMC84774
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
AID - 10.1128/MCB.19.11.7577 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Nov;19(11):7577-88. doi: 10.1128/MCB.19.11.7577.