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

Tsutomu Oshima, Eiki Yamasaki, Tadashi Ogishima, Koh Ichi Kadowaki, Akio Ito, Sakae Kitada

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)755-761
Number of pages7
JournalBiochemical Journal
Volume385
Issue number3
DOIs
Publication statusPublished - Feb 1 2005

Fingerprint

Polyproteins
Processing
Mitochondria
Succinate Dehydrogenase
mitochondrial processing peptidase
ribosomal protein S14
Mitochondrial Proteins
Nuclear Proteins
Cytosol
Yeast
Yeasts
Membranes
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase. / Oshima, Tsutomu; Yamasaki, Eiki; Ogishima, Tadashi; Kadowaki, Koh Ichi; Ito, Akio; Kitada, Sakae.

In: Biochemical Journal, Vol. 385, No. 3, 01.02.2005, p. 755-761.

Research output: Contribution to journalArticle

Oshima, Tsutomu ; Yamasaki, Eiki ; Ogishima, Tadashi ; Kadowaki, Koh Ichi ; Ito, Akio ; Kitada, Sakae. / Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase. In: Biochemical Journal. 2005 ; Vol. 385, No. 3. pp. 755-761.
@article{a4d21e97c99a42a4a17a9cc4d438cf26,
title = "Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase",
abstract = "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.",
author = "Tsutomu Oshima and Eiki Yamasaki and Tadashi Ogishima and Kadowaki, {Koh Ichi} and Akio Ito and Sakae Kitada",
year = "2005",
month = "2",
day = "1",
doi = "10.1042/BJ20041396",
language = "English",
volume = "385",
pages = "755--761",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

TY - JOUR

T1 - Recognition and processing of a nuclear-encoded polyprotein precursor by mitochondrial processing peptidase

AU - Oshima, Tsutomu

AU - Yamasaki, Eiki

AU - Ogishima, Tadashi

AU - Kadowaki, Koh Ichi

AU - Ito, Akio

AU - Kitada, Sakae

PY - 2005/2/1

Y1 - 2005/2/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=13444302475&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=13444302475&partnerID=8YFLogxK

U2 - 10.1042/BJ20041396

DO - 10.1042/BJ20041396

M3 - Article

C2 - 15458388

AN - SCOPUS:13444302475

VL - 385

SP - 755

EP - 761

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -