Proteomic Analysis of the 26S Proteasome Reveals Its Direct Interaction with Transit Peptides of Plastid Protein Precursors for Their Degradation-Reference-Cited by-同舟云学术

Proteomic Analysis of the 26S Proteasome Reveals Its Direct Interaction with Transit Peptides of Plastid Protein Precursors for Their Degradation

Published:2014-06-04 Issue:7 Volume:13 Page:3223-3230
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Sako Kaori¹,Yanagawa Yuki²,Kanai Tomoyuki³,Sato Takeo³,Seki Motoaki¹,Fujiwara Masayuki⁴,Fukao Yoichiro⁴,Yamaguchi Junji³

Affiliation:

1. Plant Genomic Network Research Team, RIKEN Center for Sustainable Resource Science, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan

2. Plant-Microbe Interaction Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan

3. Faculty of Advanced Life Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan

4. Plant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr401245g

Reference41 articles.

1. The ubiquitin–26S proteasome system at the nexus of plant biology

2. Structure of 20S proteasome from yeast at 2.4Å resolution

3. Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution

4. Proteasomes and their kin: proteases in the machine age

5. Docking of the Proteasomal ATPases' Carboxyl Termini in the 20S Proteasome's α Ring Opens the Gate for Substrate Entry

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