scholarly journals High molecular weight complex of tyrosyl-tRNA synthetase from bovine liver

1991 ◽  
Vol 7 (1) ◽  
pp. 63-69 ◽  
Author(s):  
D. V. Gnatenko ◽  
A. I. Kornelyuk ◽  
I. V. Kurochkin ◽  
G. H. Matsuka
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Bovine Liver ◽  
Trna Synthetase ◽  
High Molecular Weight Complex

P4-129 Genetic study of APH-1 and PEN-2, components of presenilin high molecular weight complex

2004 ◽  
Vol 25 ◽  
pp. S512
Author(s):  
Toshitaka Kawarai ◽  
Antonio Orlacchio ◽  
Ekaterina Rogaeva ◽  
Susan Ling ◽  
Hiroshi Hasegawa ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Genetic Study ◽  
High Molecular Weight Complex

The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins

1992 ◽  
Vol 12 (11) ◽  
pp. 4937-4945
Author(s):  
J Wang ◽  
N Suzuki ◽  
T Kataoka
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Adenylyl Cyclase ◽  
High Molecular Weight ◽  
Size Difference ◽  
Missense Mutations ◽  
Ras Proteins ◽  
High Molecular Weight Complex ◽  
Ras Protein ◽  
Dependent Activity

In the yeast Saccharomyces cerevisiae, adenylyl cyclase is regulated by RAS proteins. We show here that the yeast adenylyl cyclase forms at least two high-molecular-weight complexes, one with the RAS protein-dependent adenylyl cyclase activity and the other with the Mn(2+)-dependent activity, which are separable by their size difference. The 70-kDa adenylyl cyclase-associated protein (CAP) existed in the former complex but not in the latter. Missense mutations in conserved motifs of the leucine-rich repeats of the catalytic subunit of adenylyl cyclase abolished the RAS-dependent activity, which was accompanied by formation of a very high molecular weight complex having the Mn(2+)-dependent activity. Contrary to previous results, disruption of the gene encoding CAP did not alter the extent of RAS protein-dependent activation of adenylyl cyclase, while a concomitant decrease in the size of the RAS-responsive complex was observed. These results indicate that CAP is not essential for interaction of the yeast adenylyl cyclase with RAS proteins even though it is an inherent component of the RAS-responsive adenylyl cyclase complex.

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