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Title: RAP80 binds p32 to preserve the functional integrity of mitochondria

Abstract

RAP80, a member of the BRCA1-A complex, is a well-known crucial regulator of cell cycle checkpoint and DNA damage repair in the nucleus. However, it is still unclear whether Rap80 localizes to another region outside the nucleus and plays different roles with its partners. Here, we found mitochondrial p32 as a novel binding partner of RAP80 by using yeast two-hybrid screening. RAP80 directly binds the internal region of p32 through its arginine rich C-terminal domain. Based on the interaction, we showed that a subset of RAP80 localizes to mitochondria where p32 exists. Loss of function study revealed that RAP80 deficiency reduces the protein level of p32 and p32 dependent mitochondrial translating proteins such as Rieske and COX1. As a result, mitochondrial membrane potential and oxygen consumption are reduced in RAP80 knockdown cells, indicating mitochondrial dysfunction. Our study identifies a novel interaction between RAP80 and p32, which is important for preserving intact mitochondrial function. - Highlights: • RAP80 binds p32 through its arginine rich C-terminal region. • The loss of RAP80 expression reduces the protein level of p32. • The RAP80-p32 interaction is essential for maintaining the integrity of mitochondrial function.

Authors:
 [1]; ; ; ; ; ;  [2];  [1];  [2]
  1. Department of Biological Science, Sungkyunkwan University (SKKU), Suwon 440-746 (Korea, Republic of)
  2. Graduate School of Analytical Science and Technology (GRAST), Chungnam National University, Daejeon, 305-764 (Korea, Republic of)
Publication Date:
OSTI Identifier:
22719110
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 492; Journal Issue: 3; Other Information: Copyright (c) 2017 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ARGININE; CELL CYCLE; DNA; DNA DAMAGES; GLYCOLYSIS; HYBRIDIZATION; MITOCHONDRIA; PROTEINS; YEASTS

Citation Formats

Chung, Hee Jin, Korm, Sovannarith, Lee, Se-in, Phorl, Sophors, Noh, Solhee, Han, Miae, Naskar, Rema, Kim, Hongtae, and Lee, Joo-Yong. RAP80 binds p32 to preserve the functional integrity of mitochondria. United States: N. p., 2017. Web. doi:10.1016/J.BBRC.2017.08.077.
Chung, Hee Jin, Korm, Sovannarith, Lee, Se-in, Phorl, Sophors, Noh, Solhee, Han, Miae, Naskar, Rema, Kim, Hongtae, & Lee, Joo-Yong. RAP80 binds p32 to preserve the functional integrity of mitochondria. United States. doi:10.1016/J.BBRC.2017.08.077.
Chung, Hee Jin, Korm, Sovannarith, Lee, Se-in, Phorl, Sophors, Noh, Solhee, Han, Miae, Naskar, Rema, Kim, Hongtae, and Lee, Joo-Yong. Sat . "RAP80 binds p32 to preserve the functional integrity of mitochondria". United States. doi:10.1016/J.BBRC.2017.08.077.
@article{osti_22719110,
title = {RAP80 binds p32 to preserve the functional integrity of mitochondria},
author = {Chung, Hee Jin and Korm, Sovannarith and Lee, Se-in and Phorl, Sophors and Noh, Solhee and Han, Miae and Naskar, Rema and Kim, Hongtae and Lee, Joo-Yong},
abstractNote = {RAP80, a member of the BRCA1-A complex, is a well-known crucial regulator of cell cycle checkpoint and DNA damage repair in the nucleus. However, it is still unclear whether Rap80 localizes to another region outside the nucleus and plays different roles with its partners. Here, we found mitochondrial p32 as a novel binding partner of RAP80 by using yeast two-hybrid screening. RAP80 directly binds the internal region of p32 through its arginine rich C-terminal domain. Based on the interaction, we showed that a subset of RAP80 localizes to mitochondria where p32 exists. Loss of function study revealed that RAP80 deficiency reduces the protein level of p32 and p32 dependent mitochondrial translating proteins such as Rieske and COX1. As a result, mitochondrial membrane potential and oxygen consumption are reduced in RAP80 knockdown cells, indicating mitochondrial dysfunction. Our study identifies a novel interaction between RAP80 and p32, which is important for preserving intact mitochondrial function. - Highlights: • RAP80 binds p32 through its arginine rich C-terminal region. • The loss of RAP80 expression reduces the protein level of p32. • The RAP80-p32 interaction is essential for maintaining the integrity of mitochondrial function.},
doi = {10.1016/J.BBRC.2017.08.077},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 492,
place = {United States},
year = {2017},
month = {10}
}