scholarly journals New Alternatively Spliced Form of Galectin-3, a Member of the β-Galactoside-binding Animal Lectin Family, Contains a Predicted Transmembrane-spanning Domain and a Leucine Zipper Motif

2002 ◽  
Vol 277 (21) ◽  
pp. 18840-18848 ◽  
Author(s):  
Jeff P. Gorski ◽  
Fu-Tong Liu ◽  
Antonio Artigues ◽  
Leonardo F. Castagna ◽  
Philip Osdoby
Genetics ◽  
1997 ◽  
Vol 146 (3) ◽  
pp. 859-869 ◽  
Author(s):  
Patrick J Ferris ◽  
Ursula W Goodenough

Diploid cells of Chlamydomonas reinhardtii that are heterozygous at the mating-type locus (mt  +/mt  –) differentiate as minus gametes, a phenomenon known as minus dominance. We report the cloning and characterization of a gene that is necessary and sufficient to exert this minus dominance over the plus differentiation program. The gene, called mid, is located in the rearranged (R) domain of the mt  – locus, and has duplicated and transposed to an autosome in a laboratory strain. The imp11 mt  – mutant, which differentiates as a fusion-incompetent plus gamete, carries a point mutation in mid. Like the fus1 gene in the mt  + locus, mid displays low codon bias compared with other nuclear genes. The mid sequence carries a putative leucine zipper motif, suggesting that it functions as a transcription factor to switch on the minus program and switch off the plus program of gametic differentiation. This is the first sex-determination gene to be characterized in a green organism.


1995 ◽  
Vol 15 (7) ◽  
pp. 3759-3766 ◽  
Author(s):  
N Takamatsu ◽  
H Kanda ◽  
I Tsuchiya ◽  
S Yamada ◽  
M Ito ◽  
...  

SRY-related cDNA encoding a protein with a high-mobility-group (HMG) box and a leucine zipper motif, which was designated SOX-LZ, was isolated from a rainbow trout testis cDNA library. Comparison of this cDNA with the mouse homologous cDNA isolated from a testis cDNA library exhibits an overall amino acid sequence identity of 77%, which is in striking contrast to the abrupt loss of amino acid sequence homology outside the HMG box found among mammalian SRY genes. In both rainbow trout and mice, Northern (RNA) blot analyses have revealed the presence of a testis-specific 3-kb-long SOX-LZ mRNA, and this transcript appeared coincidentally with the protamine mRNA, suggesting its expression in the germ line. A recombinant HMG box region protein encoded by SOX-LZ could bind strongly with an oligonucleotide containing an AACAAT sequence, which is also recognized by mouse Sry and Sox-5. Upon cotransfection into CHO cells, SOX-LZ transactivated transcription through its binding motif when the region including the leucine zipper motif was deleted [SOX-LZ (D105-356)]; however, the intact SOX-LZ failed to transactivate. The intact SOX-LZ could form homodimers through the leucine zipper, which resulted in inhibition of DNA binding by the HMG box, while SOX-LZ (D105-356), which was incapable of dimerization, showed specific binding with the AACAAT sequence. Thus, the repressed transactivation of the intact SOX-LZ in CHO cells was primarily attributable to the low level of DNA binding of SOX-LZ homodimers.


Nature ◽  
1989 ◽  
Vol 340 (6229) ◽  
pp. 103-103 ◽  
Author(s):  
KEN McCoRMACK ◽  
JAMES T. CAMPANELLI ◽  
MANI RAMASWAMI ◽  
MATHEW K. MATHEW ◽  
MARK A. TANOUYE ◽  
...  

1993 ◽  
Vol 13 (11) ◽  
pp. 6711-6722 ◽  
Author(s):  
G A Rodrigues ◽  
M Park

Oncogenic activation of the met (hepatocyte growth factor/scatter factor) receptor tyrosine kinase involves a genomic rearrangement that generates a hybrid protein containing tpr-encoded sequences at its amino terminus fused directly to the met-encoded receptor kinase domain. Deletion of Tpr sequences abolishes the transforming ability of this protein, implicating this region in oncogenic activation. We demonstrate, by site-directed mutagenesis and coimmunoprecipitation experiments, that a leucine zipper motif within Tpr mediates dimerization of the tpr-met product and is essential for the transforming activity of the met oncogene. By analogy with ligand-stimulated activation of receptor tyrosine kinases, we propose that constitutive dimerization mediated by a leucine zipper motif within Tpr is responsible for oncogenic activation of the Met kinase. The possibility that this mechanism of activation represents a paradigm for a class of receptor tyrosine kinase oncogenes activated by DNA rearrangement is discussed.


2000 ◽  
Vol 275 (35) ◽  
pp. 26994-26999
Author(s):  
Murali Chiravuri ◽  
Henry Lee ◽  
Suzanne L. Mathieu ◽  
Brigitte T. Huber

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