RNA tertiary interactions in the large ribosomal subunit: The A-minor motif

Author(s):  
Poul Nissen ◽  
Joseph A. Ippolito ◽  
Nenad Ban ◽  
Peter B. Moore ◽  
Thomas A. Steitz

2001 ◽  
Vol 98 (9) ◽  
pp. 4899-4903 ◽  
Author(s):  
P. Nissen ◽  
J. A. Ippolito ◽  
N. Ban ◽  
P. B. Moore ◽  
T. A. Steitz




1988 ◽  
Vol 263 (19) ◽  
pp. 9094-9101 ◽  
Author(s):  
M Remacha ◽  
M T Sáenz-Robles ◽  
M D Vilella ◽  
J P Ballesta


Cell ◽  
2001 ◽  
Vol 107 (5) ◽  
pp. 679-688 ◽  
Author(s):  
Joerg Harms ◽  
Frank Schluenzen ◽  
Raz Zarivach ◽  
Anat Bashan ◽  
Sharon Gat ◽  
...  


2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Sunny Sharma ◽  
Johannes David Hartmann ◽  
Peter Watzinger ◽  
Arvid Klepper ◽  
Christian Peifer ◽  
...  


Author(s):  
Anders Liljas ◽  
Suparna Sanyal

Abstract The large ribosomal subunit has a distinct feature, the stalk, extending outside the ribosome. In bacteria it is called the L12 stalk. The base of the stalk is protein uL10 to which two or three dimers of proteins bL12 bind. In archea and eukarya P1 and P2 proteins constitute the stalk. All these extending proteins, that have a high degree of flexibility due to a hinge between their N- and C-terminal parts, are essential for proper functionalization of some of the translation factors. The role of the stalk proteins has remained enigmatic for decades but is gradually approaching an understanding. In this review we summarise the knowhow about the structure and function of the ribosomal stalk till date starting from the early phase of ribosome research.



Sign in / Sign up

Export Citation Format

Share Document