scholarly journals Hammerhead Ribozyme Mechanism:  A Ribonucleotide 5‘ to the Substrate Cleavage Site Is Not Essential

Biochemistry ◽  
2000 ◽  
Vol 39 (3) ◽  
pp. 624-624
Author(s):  
Anilkumar R. Kore ◽  
Fritz Eckstein
Keyword(s):  
Cleavage Site ◽  
Hammerhead Ribozyme ◽  
Substrate Cleavage

Structural Variation Induced by Different Nucleotides at the Cleavage Site of the Hammerhead Ribozyme†

Biochemistry ◽  
1998 ◽  
Vol 37 (12) ◽  
pp. 4034-4044 ◽  
Author(s):  
Jean-Pierre Simorre ◽  
Pascale Legault ◽  
Narayan Baidya ◽  
Olke C. Uhlenbeck ◽  
Lara Maloney ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Structural Variation ◽  
Hammerhead Ribozyme

scholarly journals Cohesin cleavage by separase is enhanced by a substrate motif distinct from the cleavage site

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Laura E. Rosen ◽  
Joseph E. Klebba ◽  
Jonathan B. Asfaha ◽  
Chloe M. Ghent ◽  
Melody G. Campbell ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Chromosome Segregation ◽  
Cysteine Protease ◽  
Active Site ◽  
Cleavage Site ◽  
Specific Substrate ◽  
Substrate Docking ◽  
Substrate Cleavage ◽  
Docking Interaction ◽  
Substrate Motif

AbstractChromosome segregation begins when the cysteine protease, separase, cleaves the Scc1 subunit of cohesin at the metaphase-to-anaphase transition. Separase is inhibited prior to metaphase by the tightly bound securin protein, which contains a pseudosubstrate motif that blocks the separase active site. To investigate separase substrate specificity and regulation, here we develop a system for producing recombinant, securin-free human separase. Using this enzyme, we identify an LPE motif on the Scc1 substrate that is distinct from the cleavage site and is required for rapid and specific substrate cleavage. Securin also contains a conserved LPE motif, and we provide evidence that this sequence blocks separase engagement of the Scc1 LPE motif. Our results suggest that rapid cohesin cleavage by separase requires a substrate docking interaction outside the active site. This interaction is blocked by securin, providing a second mechanism by which securin inhibits cohesin cleavage.

A Reappraisal, Based on31P NMR, of the Direct Coordination of a Metal Ion with the Phosphoryl Oxygen at the Cleavage Site of a Hammerhead Ribozyme

2002 ◽  
Vol 124 (28) ◽  
pp. 8230-8236 ◽  
Author(s):  
Ken-ichi Suzumura ◽  
Koichi Yoshinari ◽  
Yoshiyuki Tanaka ◽  
Yasuomi Takagi ◽  
Yasuhiro Kasai ◽  
...  
Keyword(s):  
Cleavage Site ◽  
Metal Ion ◽  
Hammerhead Ribozyme ◽  
Phosphoryl Oxygen

scholarly journals The Role of the Membrane-spanning Domain of Type I Signal Peptidases in Substrate Cleavage Site Selection

2000 ◽  
Vol 275 (49) ◽  
pp. 38813-38822 ◽  
Author(s):  
Joseph L. Carlos ◽  
Mark Paetzel ◽  
Greg Brubaker ◽  
Andrew Karla ◽  
Christopher M. Ashwell ◽  
...  
Keyword(s):  
Site Selection ◽  
Cleavage Site ◽  
Type I ◽  
Substrate Cleavage ◽  
Signal Peptidases ◽  
Membrane Spanning

scholarly journals The Identity of the Nucleophile Substitution May Influence Metal Interactions with the Cleavage Site of the Minimal Hammerhead Ribozyme

Biochemistry ◽  
2009 ◽  
Vol 48 (44) ◽  
pp. 10654-10664 ◽  
Author(s):  
Edith M. Osborne ◽  
W. Luke Ward ◽  
Max Z. Ruehle ◽  
Victoria J. DeRose
Keyword(s):  
Cleavage Site ◽  
Hammerhead Ribozyme ◽  
Metal Interactions
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