scholarly journals Complementation of RNA Binding Site Mutations in MS2 Coat Protein Heterodimers

1996 ◽  
Vol 24 (12) ◽  
pp. 2352-2359 ◽  
Author(s):  
D. S. Peabody ◽  
F. Lim
Biochemistry ◽  
1987 ◽  
Vol 26 (6) ◽  
pp. 1563-1568 ◽  
Author(s):  
Paul J. Romaniuk ◽  
Peggy Lowary ◽  
Huey Nan Wu ◽  
Gary Stormo ◽  
Olke C. Uhlenbeck

1983 ◽  
Vol 1 (2) ◽  
pp. 539-552 ◽  
Author(s):  
Olke C. Uhlenbeck ◽  
Jannette Carey ◽  
Paul J. Romaniuk ◽  
Peggy T. Lowary ◽  
Dorothy Beckett

1996 ◽  
Vol 271 (50) ◽  
pp. 31839-31845 ◽  
Author(s):  
Francis Lim ◽  
Marc Spingola ◽  
David S. Peabody

1994 ◽  
Vol 244 (1) ◽  
pp. 74-85 ◽  
Author(s):  
François Dragon ◽  
Catherine Payant ◽  
Léa Brakier-Gingras

1971 ◽  
Vol 234 (52) ◽  
pp. 273-275 ◽  
Author(s):  
M. GREEN ◽  
C. G. KURLAND

Endocrinology ◽  
2007 ◽  
Vol 149 (2) ◽  
pp. 534-543 ◽  
Author(s):  
John J. Peluso ◽  
Jonathan Romak ◽  
Xiufang Liu

Progesterone (P4) receptor membrane component-1 (PGRMC1) and its binding partner, plasminogen activator inhibitor 1 RNA binding protein (PAIRBP1) are thought to form a complex that functions as membrane receptor for P4. The present investigations confirm PGRMC1’s role in this membrane receptor complex by demonstrating that depleting PGMRC1 with PGRMC1 small interfering RNA results in a 60% decline in [3H]P4 binding and the loss of P4’s antiapoptotic action. Studies conducted on partially purified GFP-PGRMC1 fusion protein indicate that [3H]P4 specifically binds to PGRMC1 at a single site with an apparent Kd of about 35 nm. In addition, experiments using various deletion mutations reveal that the entire PGRMC1 molecule is required for maximal [3H]P4 binding and P4 responsiveness. Analysis of the binding data also suggests that the P4 binding site is within a segment of PGRMC1 that is composed of the transmembrane domain and the initial segment of the C terminus. Interestingly, PAIRBP1 appears to bind to the C terminus between amino acids 70–130, which is distal to the putative P4 binding site. Taken together, these data provide compelling evidence that PGRMC1 is the P4 binding protein that mediates P4’s antiapoptotic action. Moreover, the deletion mutation studies indicate that each domain of PGRMC1 plays an essential role in modulating PGRMC1’s capacity to both bind and respond to P4. Additional studies are required to more precisely delineate the role of each PGRMC1 domain in transducing P4’s antiapoptotic action.


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