scholarly journals Role of the Rubisco small subunit. Final report for period May 1, 1997--April 30,2000

2000 ◽  
Author(s):  
Robert J. Spreitzer
Keyword(s):  
Small Subunit ◽  
Final Report ◽  
Rubisco Small Subunit

scholarly journals Role of the Rubisco Small Subunit

2016 ◽  
Author(s):  
Robert Joseph Spreitzer
Keyword(s):  
Small Subunit ◽  
Rubisco Small Subunit

Final Report and Recommendations of the 2002 AACP Task Force on the Role of Colleges and Schools in Residency Training

2004 ◽  
Vol 68 (1) ◽  
pp. S2 ◽  
Author(s):  
Mary Lee ◽  
Marialice Bennett ◽  
Patricia Chase ◽  
Dick Gourley ◽  
Donald Letendre ◽  
...  
Keyword(s):  
Residency Training ◽  
Task Force ◽  
Final Report

Modulation of procaspase-7 self-activation by PEST amino acid residues of the N-terminal prodomain and intersubunit linker

2017 ◽  
Vol 95 (6) ◽  
pp. 634-643
Author(s):  
Juliano Alves ◽  
Miguel Garay-Malpartida ◽  
João M. Occhiucci ◽  
José E. Belizário
Keyword(s):  
Amino Acid ◽  
Large Subunit ◽  
Small Subunit ◽  
Cleavage Sites ◽  
Amino Acid Residues ◽  
Wild Type ◽  
Caspase 7 ◽  
Caspase Family ◽  
The Impact

Procaspase-7 zymogen polypeptide is composed of a short prodomain, a large subunit (p20), and a small subunit (p10) connected to an intersubunit linker. Caspase-7 is activated by an initiator caspase-8 and -9, or by autocatalysis after specific cleavage at IQAD198↓S located at the intersubunit linker. Previously, we identified that PEST regions made of amino acid residues Pro (P), Glu (E), Asp (D), Ser (S), Thr (T), Asn (N), and Gln (Q) are conserved flanking amino acid residues in the cleavage sites within a prodomain and intersubunit linker of all caspase family members. Here we tested the impact of alanine substitution of PEST amino acid residues on procaspase-7 proteolytic self-activation directly in Escherichia coli. The p20 and p10 subunit cleavage were significantly delayed in double caspase-7 mutants in the prodomain (N18A/P26A) and intersubunit linker (S199A/P201A), compared with the wild-type caspase-7. The S199A/P201A mutants effectively inhibited the p10 small subunit cleavage. However, the mutations did not change the kinetic parameters (kcat/KM) and optimal tetrapeptide specificity (DEVD) of the purified mutant enzymes. The results suggest a role of PEST-amino acid residues in the molecular mechanism for prodomain and intersubunit cleavage and caspase-7 self-activation.

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