NMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: proposal for a mechanism of HoxB1-pbx1-DNA complex assembly 1 1Edited by P. E. Wright

1999 ◽  
Vol 291 (3) ◽  
pp. 521-530 ◽  
Author(s):  
Carole Jabet ◽  
Rossitza Gitti ◽  
Michael F Summers ◽  
Cynthia Wolberger
Keyword(s):  
Homeodomain Protein ◽  
Nmr Studies ◽  
Complex Assembly ◽  
Tale Homeodomain ◽  
Dna Complex

Modulation of RXR-DNA complex assembly by DNA context

2019 ◽  
Vol 481 ◽  
pp. 44-52 ◽  
Author(s):  
Judit Osz ◽  
Alastair G. McEwen ◽  
Justine Wolf ◽  
Pierre Poussin-Courmontagne ◽  
Carole Peluso-Iltis ◽  
...  
Keyword(s):  
Complex Assembly ◽  
Dna Context ◽  
Dna Complex

NMR studies of the post-activated neocarzinostatin chromophore-DNA complex. Conformational changes induced in drug and DNA

1995 ◽  
Vol 3 (6) ◽  
pp. 795-809 ◽  
Author(s):  
Xiaolian Gao ◽  
Adonis Stassinopoulos ◽  
Juan Gu ◽  
Irving H. Goldberg
Keyword(s):  
Conformational Changes ◽  
Nmr Studies ◽  
Dna Complex

scholarly journals The TALE Homeodomain Protein Pbx2 Is Not Essential for Development and Long-Term Survival

2004 ◽  
Vol 24 (12) ◽  
pp. 5324-5331 ◽  
Author(s):  
Licia Selleri ◽  
Jorge DiMartino ◽  
Jan van Deursen ◽  
Andrea Brendolan ◽  
Mrinmoy Sanyal ◽  
...  
Keyword(s):  
Embryonic Development ◽  
Late Gestation ◽  
Homeodomain Protein ◽  
Mammalian Development ◽  
Term Survival ◽  
Long Term Survival ◽  
Embryonic Tissues ◽  
Adult Mice ◽  
Tale Homeodomain

ABSTRACT Pbx2 is one of four mammalian genes that encode closely related TALE homeodomain proteins, which serve as DNA binding partners for a subset of Hox transcription factors. The expression and contributions of Pbx2 to mammalian development remain undefined, in contrast to the essential roles recently established for family members Pbx1 and Pbx3. Here we report that Pbx2 is widely expressed during embryonic development, particularly in neural and epithelial tissues during late gestation. Despite wide Pbx2 expression, mice homozygous mutant for Pbx2 are born at the expected Mendelian frequencies and exhibit no detectable abnormalities in development and organogenesis or reduction of long-term survival. The lack of an apparent phenotype in Pbx2− /− mice likely reflects functional redundancy, since the Pbx2 protein is present at considerably lower levels than comparable isoforms of Pbx1 and/or Pbx3 in embryonic tissues. In postnatal bone marrow and thymus, however, Pbx2 is the predominant high-molecular-weight (MW)-isoform Pbx protein detectable by immunoblotting. Nevertheless, the absence of Pbx2 has no measurable effect on steady-state hematopoiesis or immune function in adult mice, suggesting possible compensation by low-MW-isoform Pbx proteins present in these tissues. We conclude that the roles of Pbx2 in murine embryonic development, organogenesis, hematopoiesis, immune responses, and long-term survival are not essential.

Kinetic Analysis of the Interaction ofMos1Transposase with its Inverted Terminal Repeats Reveals New Insight into the Protein-DNA Complex Assembly

ChemBioChem ◽  
2014 ◽  
Vol 16 (1) ◽  
pp. 140-148
Author(s):  
Charles Esnault ◽  
Jérôme Jaillet ◽  
Nicolas Delorme ◽  
Nicolas Bouchet ◽  
Sylvaine Renault ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Complex Assembly ◽  
Inverted Terminal Repeats ◽  
Terminal Repeats ◽  
Dna Complex ◽  
Insight Into

A cellular factor binds to the herpes simplex virus type 1 transactivator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1

1990 ◽  
Vol 10 (9) ◽  
pp. 4974-4977
Author(s):  
P Xiao ◽  
J P Capone
Keyword(s):  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Complex Assembly ◽  
Cellular Factor ◽  
Target Dna ◽  
Dependent Protein ◽  
Simplex Virus ◽  
Dna Complex

The herpes simplex virus transactivator Vmw65 assembles into a multicomponent protein-DNA complex along with the octamer binding protein Oct-1. Using affinity chromatography on columns conjugated with purified Vmw65 fusion protein expressed in Escherichia coli, we demonstrate that a cellular factor, distinct from Oct-1, binds to Vmw65 in the absence of target DNA and is necessary for Vmw65-mediated complex assembly with Oct-1.

Synergistic roles of homeodomain proteins UNC-62 homothorax and MLS-2 HMX/NKX in the specification of olfactory neurons in Caenorhabditis elegans

Genetics ◽  
2021 ◽  
Author(s):  
Yi-Wen Hsieh ◽  
Rui Xiong ◽  
Chiou-Fen Chuang
Keyword(s):  
Transcription Factor ◽  
Caenorhabditis Elegans ◽  
Incomplete Penetrance ◽  
Homeodomain Protein ◽  
Homeodomain Proteins ◽  
Complete Penetrance ◽  
Late Embryogenesis ◽  
Tale Homeodomain ◽  
Null Mutants

Abstract General identity of the Caenorhabditis elegans AWC olfactory neuron pair is specified by the OTX/OTD transcription factor CEH-36 and the HMG-box transcription factor SOX-2, followed by asymmetrical differentiation of the pair into two distinct subtypes, default AWCOFF and induced AWCON, through a stochastic signaling event. The HMX/NKX transcription factor MLS-2 regulates the expression of ceh-36 to specify general AWC identity. However, general AWC identity is lost in only one of the two AWC cells in the majority of mls-2 null mutants displaying defective general AWC identity, suggesting that additional transcription factors have a partially overlapping role with MLS-2 in the specification of general AWC identity. Here we identify a role of unc-62, encoding a homothorax/Meis/TALE homeodomain protein, in the specification of general AWC identity. As in mls-2 null mutants, unc-62 null mutants showed an incomplete penetrance in loss of general AWC identity. However, unc-62; mls-2 double mutants display a nearly complete penetrance of identity loss in both AWC cells. Thus, unc-62 and mls-2 have a partially overlapping function in the specification of general AWC identity. Furthermore, our genetic results suggest that mls-2 and unc-62 act cell autonomously in promoting the AWCON subtype. Together, our findings reveal the sequential roles of the unc-62 and mls-2 pair in AWC development, specification of general AWC identity in early embryogenesis and asymmetric differentiation of AWC subtypes in late embryogenesis.

scholarly journals A cellular factor binds to the herpes simplex virus type 1 transactivator Vmw65 and is required for Vmw65-dependent protein-DNA complex assembly with Oct-1.

1990 ◽  
Vol 10 (9) ◽  
pp. 4974-4977 ◽  
Author(s):  
P Xiao ◽  
J P Capone
Keyword(s):  
Escherichia Coli ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Complex Assembly ◽  
Cellular Factor ◽  
Target Dna ◽  
Dependent Protein ◽  
Simplex Virus ◽  
Dna Complex

The herpes simplex virus transactivator Vmw65 assembles into a multicomponent protein-DNA complex along with the octamer binding protein Oct-1. Using affinity chromatography on columns conjugated with purified Vmw65 fusion protein expressed in Escherichia coli, we demonstrate that a cellular factor, distinct from Oct-1, binds to Vmw65 in the absence of target DNA and is necessary for Vmw65-mediated complex assembly with Oct-1.

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