scholarly journals Determination of the Cleavage Site of the Presequence by Mitochondrial Processing Peptidase on the Substrate Binding Scaffold and the Multiple Subsites inside a Molecular Cavity

2002 ◽  
Vol 278 (3) ◽  
pp. 1879-1885 ◽  
Author(s):  
Sakae Kitada ◽  
Eiki Yamasaki ◽  
Katsuhiko Kojima ◽  
Akio Ito
Keyword(s):  
Cleavage Site ◽  
Substrate Binding ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase

Substrate Binding Changes Conformation of the α-, but Not the β-Subunit of Mitochondrial Processing Peptidase

2001 ◽  
Vol 385 (2) ◽  
pp. 392-396 ◽  
Author(s):  
Oleksandr Gakh ◽  
Tomas Obsil ◽  
Jiri Adamec ◽  
Jaroslav Spizek ◽  
Evzen Amler ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Β Subunit ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase

scholarly journals Cooperative Formation of a Substrate Binding Pocket by α- and β-Subunits of Mitochondrial Processing Peptidase

1998 ◽  
Vol 273 (49) ◽  
pp. 32542-32546 ◽  
Author(s):  
Katsuhiko Kojima ◽  
Sakae Kitada ◽  
Kunitoshi Shimokata ◽  
Tadashi Ogishima ◽  
Akio Ito
Keyword(s):  
Substrate Binding ◽  
Binding Pocket ◽  
Substrate Binding Pocket ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase ◽  
Α And Β Subunits

scholarly journals Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase

2005 ◽  
Vol 385 (3) ◽  
pp. 755-761 ◽  
Author(s):  
Tsutomu OSHIMA ◽  
Eiki YAMASAKI ◽  
Tadashi OGISHIMA ◽  
Koh-ichi KADOWAKI ◽  
Akio ITO ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Succinate Dehydrogenase ◽  
Cleavage Site ◽  
Essential Role ◽  
Mitochondrial Matrix ◽  
Inner Membrane ◽  
Mitochondrial Processing Peptidase ◽  
Large N ◽  
Processing Peptidase ◽  
Polyprotein Precursor

The nuclear-encoded protein RPS14 (ribosomal protein S14) of rice mitochondria is synthesized in the cytosol as a polyprotein consisting of a large N-terminal domain comprising preSDHB (succinate dehydrogenase B precursor) and the C-terminal RPS14. After the preSDHB–RPS14 polyprotein is transported into the mitochondrial matrix, the protein is processed into three peptides: the N-terminal prepeptide, the SDHB domain and the C-terminal mature RPS14. Here we report that the general MPP (mitochondrial processing peptidase) plays an essential role in processing of the polyprotein. Purified yeast MPP cleaved both the N-terminal presequence and the connector region between SDHB and RPS14. Moreover, the connector region was processed more rapidly than the presequence. When the site of cleavage between SDHB and RPS14 was determined, it was located in an MPP processing motif that has also been shown to be present in the N-terminal presequence. Mutational analyses around the cleavage site in the connector region suggested that MPP interacts with multiple sites in the region, possibly in a similar manner to the interaction with the N-terminal presequence. In addition, MPP preferentially recognized the unfolded structure of preSDHB–RPS14. In mitochondria, MPP may recognize the stretched polyprotein during passage of the precursor through the translocational apparatus in the inner membrane, and cleave the connecting region between the SDHB and RPS14 domains even before processing of the presequence.

scholarly journals Glutamate Residues Required for Substrate Binding and Cleavage Activity in Mitochondrial Processing Peptidase

1998 ◽  
Vol 273 (49) ◽  
pp. 32547-32553 ◽  
Author(s):  
Sakae Kitada ◽  
Katsuhiko Kojima ◽  
Kunitoshi Shimokata ◽  
Tadashi Ogishima ◽  
Akio Ito
Keyword(s):  
Substrate Binding ◽  
Cleavage Activity ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase

scholarly journals Maturation of Mitochondrially Targeted Prx V Involves a Second Cleavage by Mitochondrial Intermediate Peptidase That Is Sensitive to Inhibition by H2O2

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 346
Author(s):  
Juhyun Sim ◽  
Jiyoung Park ◽  
Hyun Ae Woo ◽  
Sue Goo Rhee
Keyword(s):  
Short Form ◽  
Mitochondrial Matrix ◽  
Mitochondrial Processing Peptidase ◽  
Mouse Tissues ◽  
N Terminus ◽  
Mitochondrial Intermediate Peptidase ◽  
Subsequent Degradation ◽  
Processing Peptidase ◽  
Mitochondria Targeting ◽  
Over Time

Prx V mRNA contains two in-frame AUG codons, producing a long (L-Prx V) and short form of Prx V (S-Prx V), and mouse L-Prx V is expressed as a precursor protein containing a 49-amino acid N-terminal mitochondria targeting sequence. Here, we show that the N-terminal 41-residue sequence of L-Prx V is cleaved by mitochondrial processing peptidase (MPP) in the mitochondrial matrix to produce an intermediate Prx V (I-Prx V) with a destabilizing phenylalanine at its N-terminus, and further, that the next 8-residue sequence is cleaved by mitochondrial intermediate peptidase (MIP) to convert I-Prx V to a stabilized mature form that is identical to S-Prx V. Further, we show that when mitochondrial H2O2 levels are increased in HeLa cells using rotenone, in several mouse tissues by deleting Prx III, and in the adrenal gland by deleting Srx or by exposing mice to immobilized stress, I-Prx V accumulates transiently and mature S-Prx V levels decrease in mitochondria over time. These findings support the view that MIP is inhibited by H2O2, resulting in the accumulation and subsequent degradation of I-Prx V, identifying a role for redox mediated regulation of Prx V proteolytic maturation and expression in mitochondria.

scholarly journals Characterization of the mitochondrial processing peptidase of Neurospora crassa.

1994 ◽  
Vol 269 (7) ◽  
pp. 4959-4967 ◽  
Author(s):  
M. Arretz ◽  
H. Schneider ◽  
B. Guiard ◽  
M. Brunner ◽  
W. Neupert
Keyword(s):  
Neurospora Crassa ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase
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