Research ExplorerPublicationsRole of Pex19p in the targeting of PMP70 to peroxisome

Role of Pex19p in the targeting of PMP70 to peroxisome

Standard

Role of Pex19p in the targeting of PMP70 to peroxisome. / Kashiwayama, Yoshinori; Asahina, Kota; Shibata, Hiroyuki; Morita, Masashi; Muntau, Ania C; Roscher, Adelbert A; Wanders, Ronald J A; Shimozawa, Nobuyuki; Sakaguchi, Masao; Kato, Hiroaki; Imanaka, Tsuneo.

In: Biochim Biophys Acta, Vol. 1746, No. 2, 15.12.2005, p. 116-28.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kashiwayama, Y, Asahina, K, Shibata, H, Morita, M, Muntau, AC, Roscher, AA, Wanders, RJA, Shimozawa, N, Sakaguchi, M, Kato, H & Imanaka, T 2005, 'Role of Pex19p in the targeting of PMP70 to peroxisome', Biochim Biophys Acta, vol. 1746, no. 2, pp. 116-28. https://doi.org/10.1016/j.bbamcr.2005.10.006

APA

Kashiwayama, Y., Asahina, K., Shibata, H., Morita, M., Muntau, A. C., Roscher, A. A., Wanders, R. J. A., Shimozawa, N., Sakaguchi, M., Kato, H., & Imanaka, T. (2005). Role of Pex19p in the targeting of PMP70 to peroxisome. Biochim Biophys Acta, 1746(2), 116-28. https://doi.org/10.1016/j.bbamcr.2005.10.006

Vancouver

Kashiwayama Y, Asahina K, Shibata H, Morita M, Muntau AC, Roscher AA et al. Role of Pex19p in the targeting of PMP70 to peroxisome. Biochim Biophys Acta. 2005 Dec 15;1746(2):116-28. https://doi.org/10.1016/j.bbamcr.2005.10.006

Bibtex

@article{ca7c69ca00fe4933903fc4cb9b66b5d7,
title = "Role of Pex19p in the targeting of PMP70 to peroxisome",
abstract = "Pex19p is a protein required for the peroxisomal membrane synthesis. The 70-kDa peroxisomal membrane protein (PMP70) is synthesized on free cytosolic ribosomes and then inserted posttranslationally into peroxisomal membranes. Pex19p has been shown to play an important role in this process. Using an in vitro translation system, we investigated the role of Pex19p as a chaperone and identified the regions of PMP70 required for the interaction with Pex19p. When PMP70 was translated in the presence of purified Pex19p, a large part of PMP70 existed as soluble form and was co-immunoprecipitated with Pex19p. However, in the absence of Pex19p, PMP70 formed aggregates during translation. To identify the regions that interact with Pex19p, various truncated PMP70 were translated in the presence of Pex19p and subjected to co-immunoprecipitation. The interaction was markedly reduced by the deletion of the NH(2)-terminal 61 amino acids or the region around TMD6. Further, we expressed these deletion constructs of PMP70 in fusion with the green fluorescent protein in CHO cells. Fusion proteins lacking these Pex19p binding sites did not display any peroxisomal localization. These results suggest that Pex19p binds to PMP70 co-translationally and keeps PMP70 as a proper conformation for the localization to peroxisome.",
keywords = "ATP-Binding Cassette Transporters/chemistry, Animals, Base Sequence, Binding Sites, Biological Transport, Active, CHO Cells, Cricetinae, DNA, Complementary/genetics, Green Fluorescent Proteins/genetics, Humans, In Vitro Techniques, Membrane Proteins/chemistry, Mice, Peptide Fragments/chemistry, Peroxisomes/metabolism, Protein Binding, Protein Biosynthesis, RNA, Messenger/genetics, Recombinant Fusion Proteins/chemistry, Sequence Deletion, Solubility",
author = "Yoshinori Kashiwayama and Kota Asahina and Hiroyuki Shibata and Masashi Morita and Muntau, {Ania C} and Roscher, {Adelbert A} and Wanders, {Ronald J A} and Nobuyuki Shimozawa and Masao Sakaguchi and Hiroaki Kato and Tsuneo Imanaka",
year = "2005",
month = dec,
day = "15",
doi = "10.1016/j.bbamcr.2005.10.006",
language = "English",
volume = "1746",
pages = "116--28",
journal = "Biochim Biophys Acta",
issn = "0006-3002",
number = "2",

}

RIS

TY - JOUR

T1 - Role of Pex19p in the targeting of PMP70 to peroxisome

AU - Kashiwayama, Yoshinori

AU - Asahina, Kota

AU - Shibata, Hiroyuki

AU - Morita, Masashi

AU - Muntau, Ania C

AU - Roscher, Adelbert A

AU - Wanders, Ronald J A

AU - Shimozawa, Nobuyuki

AU - Sakaguchi, Masao

AU - Kato, Hiroaki

AU - Imanaka, Tsuneo

PY - 2005/12/15

Y1 - 2005/12/15

N2 - Pex19p is a protein required for the peroxisomal membrane synthesis. The 70-kDa peroxisomal membrane protein (PMP70) is synthesized on free cytosolic ribosomes and then inserted posttranslationally into peroxisomal membranes. Pex19p has been shown to play an important role in this process. Using an in vitro translation system, we investigated the role of Pex19p as a chaperone and identified the regions of PMP70 required for the interaction with Pex19p. When PMP70 was translated in the presence of purified Pex19p, a large part of PMP70 existed as soluble form and was co-immunoprecipitated with Pex19p. However, in the absence of Pex19p, PMP70 formed aggregates during translation. To identify the regions that interact with Pex19p, various truncated PMP70 were translated in the presence of Pex19p and subjected to co-immunoprecipitation. The interaction was markedly reduced by the deletion of the NH(2)-terminal 61 amino acids or the region around TMD6. Further, we expressed these deletion constructs of PMP70 in fusion with the green fluorescent protein in CHO cells. Fusion proteins lacking these Pex19p binding sites did not display any peroxisomal localization. These results suggest that Pex19p binds to PMP70 co-translationally and keeps PMP70 as a proper conformation for the localization to peroxisome.

AB - Pex19p is a protein required for the peroxisomal membrane synthesis. The 70-kDa peroxisomal membrane protein (PMP70) is synthesized on free cytosolic ribosomes and then inserted posttranslationally into peroxisomal membranes. Pex19p has been shown to play an important role in this process. Using an in vitro translation system, we investigated the role of Pex19p as a chaperone and identified the regions of PMP70 required for the interaction with Pex19p. When PMP70 was translated in the presence of purified Pex19p, a large part of PMP70 existed as soluble form and was co-immunoprecipitated with Pex19p. However, in the absence of Pex19p, PMP70 formed aggregates during translation. To identify the regions that interact with Pex19p, various truncated PMP70 were translated in the presence of Pex19p and subjected to co-immunoprecipitation. The interaction was markedly reduced by the deletion of the NH(2)-terminal 61 amino acids or the region around TMD6. Further, we expressed these deletion constructs of PMP70 in fusion with the green fluorescent protein in CHO cells. Fusion proteins lacking these Pex19p binding sites did not display any peroxisomal localization. These results suggest that Pex19p binds to PMP70 co-translationally and keeps PMP70 as a proper conformation for the localization to peroxisome.

KW - ATP-Binding Cassette Transporters/chemistry

KW - Animals

KW - Base Sequence

KW - Binding Sites

KW - Biological Transport, Active

KW - CHO Cells

KW - Cricetinae

KW - DNA, Complementary/genetics

KW - Green Fluorescent Proteins/genetics

KW - Humans

KW - In Vitro Techniques

KW - Membrane Proteins/chemistry

KW - Mice

KW - Peptide Fragments/chemistry

KW - Peroxisomes/metabolism

KW - Protein Binding

KW - Protein Biosynthesis

KW - RNA, Messenger/genetics

KW - Recombinant Fusion Proteins/chemistry

KW - Sequence Deletion

KW - Solubility

U2 - 10.1016/j.bbamcr.2005.10.006

DO - 10.1016/j.bbamcr.2005.10.006

M3 - SCORING: Journal article

C2 - 16344115

VL - 1746

SP - 116

EP - 128

JO - Biochim Biophys Acta

JF - Biochim Biophys Acta

SN - 0006-3002

IS - 2

ER -