The porcine gene TBP10 encodes a protein homologous to the human Tat-binding protein/26S protease subunit family

1996 ◽  
Vol 7 (3) ◽  
pp. 180-185 ◽  
Author(s):  
T. Leeb ◽  
G. Rettenberger ◽  
J. Bruch ◽  
H. Hameister ◽  
B. Brenig
Keyword(s):  
Binding Protein ◽  
Porcine Gene ◽  
26S Protease

scholarly journals Growth and developmental functions of a human immunodeficiency virus Tat-binding protein/26S protease subunit homolog from Dictyostelium discoideum.

1995 ◽  
Vol 15 (3) ◽  
pp. 1725-1736 ◽  
Author(s):  
J G Cao ◽  
R A Firtel
Keyword(s):  
Human Immunodeficiency Virus ◽  
Dictyostelium Discoideum ◽  
Binding Protein ◽  
Yeast Cells ◽  
Regulation Of Transcription ◽  
Multicellular Aggregate ◽  
Immunodeficiency Virus ◽  
Null Phenotype ◽  
Antisense Construct ◽  
26S Protease

We have characterized a newly identified gene from Dictyostelium discoideum, DdTBP alpha, that encodes a member of the family of eukaryotic proteins. These proteins contain a conserved ATPase domain, include subunits of the 26S protease subunit, and are homologous to the mammalian human immunodeficiency virus Tat-binding protein TBP1. While information indicates that some family members are involved in the regulation of transcription in mammalian and yeast cells during growth, these proteins are also involved in other cellular functions, and nothing is known about their possible function in multicellular development. The Dictyostelium DdTBP alpha gene is developmentally regulated, with its expression at the highest levels occurring during growth and early development. The gene is present in two copies in the genome. Disruption of one copy by homologous recombination leads to aberrant morphogenesis, which lasts from the formation of the first finger until the onset of culmination. The gene appears to be essential for growth since we were unable to obtain a complete null phenotype and since expression of an inducible antisense construct in the partial null background resulted in cell death. Expression of the antisense construct during development accentuated the partial null phenotype and also resulted in very abnormal fruiting bodies. Overexpression of DdTBP alpha from its own promoter leads to very large multinucleated vegetative cells when the cells are grown in suspension culture. When the cells are plated onto petri dishes in growth medium, they rapidly split into multiple cells containing one to two nuclei, in a manner similar to that of wild-type cells. Overexpressing cells are significantly delayed in forming a multicellular aggregate, but development proceeds normally once the first finger stage is reached. The results indicate that DdTBP alpha plays an important role in regulating both growth and morphogenesis in D. discoideum.

Kupffer cell activation by LPS is mediated via LPS binding protein and CD14

2001 ◽  
Vol 120 (5) ◽  
pp. A27-A27
Author(s):  
M FAN ◽  
S GOYERT ◽  
A AMINLARI ◽  
R KLEIN ◽  
L STEINSTRAESSER ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Activation ◽  
Binding Protein ◽  
Lps Binding

Annexin VI is a Ca2+-sensitive CHSP-28 binding protein present on secretory granule membranes in acini

2001 ◽  
Vol 120 (5) ◽  
pp. A336-A336
Author(s):  
G GROBLEWSKI ◽  
D THOMAS ◽  
W TAFT ◽  
K KASPAR
Keyword(s):  
Secretory Granule ◽  
Binding Protein ◽  
Annexin Vi

235: The RNA-Binding Protein IMP3: A Novel Molecular Marker Predicts Progression of Superficial (TA and T1) Urothelial Carcinomas of Bladder

2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  
Keyword(s):  
Molecular Marker ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Urothelial Carcinomas
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