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 Isolation, Characterization, and Expression of the Gene Encoding the β Subunit of the Mitochondrial Processing Peptidase fromBlastocladiella emersonii

1998 ◽  
Vol 180 (15) ◽  
pp. 3967-3972 ◽  
Author(s):  
Cíntia Renata Costa Rocha ◽  
Suely Lopes Gomes
Keyword(s):  
Genomic Library ◽  
Nucleotide Sequence Analysis ◽  
Mrna Levels ◽  
Β Subunit ◽  
Coding Region ◽  
Gene Encoding ◽  
Western Blots ◽  
Calculated Molecular Mass ◽  
Mitochondrial Processing Peptidase ◽  
Processing Peptidase

ABSTRACT A 2.3-kb BamHI-KpnI fragment was isolated from a partial genomic library and shown by nucleotide sequence analysis to contain the entire coding region of the gene encoding the β subunit of the Blastocladiella mitochondrial processing peptidase (β-MPP). The predicted β-MPP protein has 465 amino acids and a calculated molecular mass of 50.8 kDa. S1 nuclease protection assays revealed an intron, 209 bp in size, interrupting the coding region between the putative signal sequence and the mature protein. Northern blot analysis showed that β-MPP mRNA levels decrease significantly during B. emersonii sporulation, reaching basal levels in the zoospore stage. The amount of β-MPP protein, determined in Western blots, unlike its mRNA, does not vary significantly throughout the fungal life cycle.

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 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.

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