In vitro assembly of 30S ribosomal particles from precursor 16S RNA of Escherichia coli

Nature ◽  
1974 ◽  
Vol 247 (5442) ◽  
pp. 552-554 ◽  
Author(s):  
JOHN W. WIREMAN ◽  
PAUL S. SYPHERD
Biochimie ◽  
1976 ◽  
Vol 58 (8) ◽  
pp. 1007-1009 ◽  
Author(s):  
Jacques Alain Tréton ◽  
Françoise Hayes
Keyword(s):  

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1002-1011 ◽  
Author(s):  
Robert Denman ◽  
Carl Weitzmann ◽  
Philip R. Cunningham ◽  
Didier Negre ◽  
Kelvin Nurse ◽  
...  

Virology ◽  
1995 ◽  
Vol 207 (2) ◽  
pp. 486-494 ◽  
Author(s):  
Xiaoxia Zhao ◽  
James M. Fox ◽  
Norman H. Olson ◽  
Timothy S. Baker ◽  
Mark J. Young

1987 ◽  
Vol 262 (21) ◽  
pp. 10327-10334 ◽  
Author(s):  
B.E. Funnell ◽  
T.A. Baker ◽  
A. Kornberg

1999 ◽  
Vol 73 (7) ◽  
pp. 5309-5319 ◽  
Author(s):  
Timothy L. Tellinghuisen ◽  
Agnes E. Hamburger ◽  
Bonnie R. Fisher ◽  
Ralf Ostendorp ◽  
Richard J. Kuhn

ABSTRACT The production of the alphavirus virion is a multistep event requiring the assembly of the nucleocapsid core in the cytoplasm and the maturation of the glycoproteins in the endoplasmic reticulum and the Golgi apparatus. These components associate during the budding process to produce the mature virion. The nucleocapsid proteins of Sindbis virus and Ross River virus have been produced in a T7-basedEscherichia coli expression system and purified. In the presence of single-stranded but not double-stranded nucleic acid, the proteins oligomerize in vitro into core-like particles which resemble the native viral nucleocapsid cores. Despite their similarities, Sindbis virus and Ross River virus capsid proteins do not form mixed core-like particles. Truncated forms of the Sindbis capsid protein were used to establish amino acid requirements for assembly. A capsid protein starting at residue 19 [CP(19–264)] was fully competent for in vitro assembly, whereas proteins with further N-terminal truncations could not support assembly. However, a capsid protein starting at residue 32 or 81 was able to incorporate into particles in the presence of CP(19–264) or could inhibit assembly if its molar ratio relative to CP(19–264) was greater than 1:1. This system provides a basis for the molecular dissection of alphavirus core assembly.


Biochimie ◽  
1991 ◽  
Vol 73 (6) ◽  
pp. 789-796 ◽  
Author(s):  
P.R. Cunningham ◽  
R.B. Richard ◽  
C.J. Weitzmann ◽  
K. Nurse ◽  
J. Ofengand

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