Tracing foreign sequences in plant transcriptomes and genomes using OCT4, a POU domain protein

Author(s):  
Adeleh Saffar ◽  
Maryam M. Matin
Keyword(s):  
Oncogene ◽  
1997 ◽  
Vol 14 (11) ◽  
pp. 1287-1294 ◽  
Author(s):  
Suzana Atanasoski ◽  
Edgar Schreiber ◽  
Adriano Fontana ◽  
Winship Herr
Keyword(s):  

2004 ◽  
Vol 24 (7) ◽  
pp. 2944-2957 ◽  
Author(s):  
S. Molinari ◽  
F. Relaix ◽  
M. Lemonnier ◽  
B. Kirschbaum ◽  
B. Schäfer ◽  
...  

ABSTRACT Expression of the mouse cardiac actin gene depends on a distal enhancer (−7 kbp) which has been shown, in transgenic mice, to direct expression to embryonic skeletal muscle. The presence of this distal sequence is also associated with reproducible expression of cardiac actin transgenes. In differentiated skeletal muscle cells, activity of the enhancer is driven by an E box, binding MyoD family members, and by a 3′ AT-rich sequence which is in the location of a DNase I-hypersensitive site. This sequence does not bind MEF2 proteins, or other known muscle transcription factors, directly. Oct1 and Emb, a class VI POU domain protein, bind to consensus sites on the DNA, and it is the binding of Emb which is important for activity. Emb binds as a major complex with MEF2D and the histone transacetylase p300. The form of Emb present in this complex and as a major form in muscle cell extracts is longer (80 kDa) than that previously described. These results demonstrate the importance of this novel complex in the transcriptional regulation of the cardiac actin gene and suggest a potential role in chromatin remodeling associated with muscle gene activation.


1993 ◽  
Vol 13 (9) ◽  
pp. 5450-5460 ◽  
Author(s):  
H Messier ◽  
H Brickner ◽  
J Gaikwad ◽  
A Fotedar

POU domain proteins have been implicated in the regulation of a number of lineage-specific genes. Among the first POU domain proteins described were the immunoglobulin octamer-binding proteins Oct-1 and Oct-2. It was therefore of special interest when we identified a novel lymphoid POU domain protein in Southwestern (DNA-protein) screens of T-cell lambda gt11 libraries. This novel POU protein, TCF beta 1, binds in a sequence-specific manner to a critical motif in the T-cell receptor (TCR) beta enhancer. Sequence analysis revealed that TCF beta 1 represents a new class of POU domain proteins which are distantly related to other POU proteins. TCF beta 1 is encoded by multiple exons whose organization is distinct from that of other POU domain proteins. The expression of TCF beta 1 in a tissue-restricted manner and its ability to bind to multiple motifs in the TCR beta enhancer support a role in regulating TCR beta gene expression. The expression of TCF beta 1 in both B and T cells and the ability of recombinant TCF beta 1 to bind octamer and octamer-related motifs suggest that TCF beta 1 has additional roles in lymphoid cell function. The ability of TCF beta 1 to transactivate in a sequence-specific manner is consistent with a role for regulating lymphoid gene expression.


1993 ◽  
Vol 90 (22) ◽  
pp. 10841-10845 ◽  
Author(s):  
M. R. Gerrero ◽  
R. J. McEvilly ◽  
E. Turner ◽  
C. R. Lin ◽  
S. O'Connell ◽  
...  
Keyword(s):  

1989 ◽  
Vol 3 (7) ◽  
pp. 946-958 ◽  
Author(s):  
H J Mangalam ◽  
V R Albert ◽  
H A Ingraham ◽  
M Kapiloff ◽  
L Wilson ◽  
...  

1996 ◽  
Vol 38 (2) ◽  
pp. 209-221 ◽  
Author(s):  
Karl F. Malik ◽  
Jin Kim ◽  
Adam L. Hartman ◽  
Paul Kim ◽  
W. Scott Young
Keyword(s):  

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