Structure, stability, and biological activity of bacteriophage T4 gene product 9 probed with mutagenesis and monoclonal antibodies

2006 ◽  
Vol 154 (2) ◽  
pp. 122-129 ◽  
Author(s):  
Lidia P. Kurochkina ◽  
Alexandr Yu. Vishnevskiy ◽  
Lyuba V. Zhemaeva ◽  
Nina N. Sykilinda ◽  
Sergei V. Strelkov ◽  
...  
1989 ◽  
Vol 21 (4) ◽  
pp. 517-524 ◽  
Author(s):  
Akira Matsuno ◽  
Hiromi Takaimo-Ohmuro ◽  
Yoshiharu Itoh ◽  
Tetsu Matsuura ◽  
Masao Shibata ◽  
...  

2000 ◽  
Vol 301 (4) ◽  
pp. 975-985 ◽  
Author(s):  
Petr G Leiman ◽  
Victor A Kostyuchenko ◽  
Mikhail M Shneider ◽  
Lidia P Kurochkina ◽  
Vadim V Mesyanzhinov ◽  
...  

1991 ◽  
Vol 225 (3) ◽  
pp. 427-434 ◽  
Author(s):  
Andreas Gansz ◽  
Ulrich Kruse ◽  
Wolfgang Rüger

2008 ◽  
Vol 73 (9) ◽  
pp. 995-999
Author(s):  
L. P. Kurochkina ◽  
A. Yu. Vishnevskiy ◽  
V. V. Mesyanzhinov

1986 ◽  
Vol 6 (4) ◽  
pp. 1343-1348 ◽  
Author(s):  
M Hannink ◽  
D J Donoghue

The v-sis oncogene and its cellular homolog c-sis encode chain B of platelet-derived growth factor. Cells transformed by v-sis produce a platelet-derived growth factor-related molecule which is able to stimulate the platelet-derived growth factor receptor in an autocrine fashion. Site-directed mutagenesis was used to construct several mutations which substitute charged residues for hydrophobic residues in the proposed signal sequence of the v-sis gene product. Two of these mutations resulted in the synthesis of altered v-sis gene products with an unexpected nuclear location and a loss of biological activity. We also report here the intracellular localization of the v-sis gene product to the endoplasmic reticulum-Golgi compartment, where signal sequence cleavage and N-linked glycosylation occur. The v-sis gene product contains no transmembrane regions, as it is completely protected within isolated microsomes from trypsin proteolysis. Site-directed mutagenesis was also used to alter a proposed proteolytic processing site in the v-sis gene product. This mutant v-sis gene, which encodes Asn-Ser in place of Lys-Arg at residues 110 to 111, was found to retain full biological activity.


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