Glu191 and Asp195 in Rat Mitochondrial Processing Peptidase β Subunit Are Involved in Effective Cleavage of Precursor Protein through Interaction with the Proximal Arginine

2001 ◽  
Vol 287 (3) ◽  
pp. 594-599 ◽  
Author(s):  
Sakae Kitada ◽  
Katsuhiko Kojima ◽  
Akio Ito
Keyword(s):  
Precursor Protein ◽  
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.

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 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 Proteomic profiling of the mitochondrial ribosome identifies Atp25 as a composite mitochondrial precursor protein

2016 ◽  
Vol 27 (20) ◽  
pp. 3031-3039 ◽  
Author(s):  
Michael W. Woellhaf ◽  
Frederik Sommer ◽  
Michael Schroda ◽  
Johannes M. Herrmann
Keyword(s):  
Precursor Protein ◽  
Ribosomal Biogenesis ◽  
Proteomic Profiling ◽  
Mitochondrial Translation ◽  
Bacterial Ribosome ◽  
Mitochondrial Ribosome ◽  
Translation Apparatus ◽  
The Matrix ◽  
Processing Peptidase ◽  
And Function

Whereas the structure and function of cytosolic ribosomes are well characterized, we only have a limited understanding of the mitochondrial translation apparatus. Using SILAC-based proteomic profiling, we identified 13 proteins that cofractionated with the mitochondrial ribosome, most of which play a role in translation or ribosomal biogenesis. One of these proteins is a homologue of the bacterial ribosome-silencing factor (Rsf). This protein is generated from the composite precursor protein Atp25 upon internal cleavage by the matrix processing peptidase MPP, and in this respect, it differs from all other characterized mitochondrial proteins of baker’s yeast. We observed that cytosolic expression of Rsf, but not of noncleaved Atp25 protein, is toxic. Our results suggest that eukaryotic cells face the challenge of avoiding negative interference from the biogenesis of their two distinct translation machineries.

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