MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus

Author:

Fujiwara Naoko1,Shigemoto Maki1,Hirayama Mizuki1,Fujita Ken-ichi12,Seno Shigeto3,Matsuda Hideo3,Nagahama Masami4,Masuda Seiji1567ORCID

Affiliation:

1. Graduate School of Biostudies, Kyoto University , Kyoto , Kyoto  606-8502, Japan

2. Division of Gene Expression Mechanism, Institute for Comprehensive Medical Science, Fujita Health University , Toyoake , Aichi  470-1192, Japan

3. Graduate School of Information Science and Technology, Osaka University , Suita , Osaka  565-0871, Japan

4. Laboratory of Molecular and Cellular Biochemistry, Meiji Pharmaceutical University , Kiyose , Tokyo  204-8588, Japan

5. Department of Food Science and Nutrition, Faculty of Agriculture Kindai University , Nara , Nara  631-8505, Japan

6. Agricultural Technology and Innovation Research Institute, Kindai University , Nara , Nara  631-8505, Japan

7. Antiaging center, Kindai University , Higashiosaka , Osaka  577-8502, Japan

Abstract

Abstract Recent in vitro reconstitution analyses have proven that the physical interaction between the exosome core and MTR4 helicase, which promotes the exosome activity, is maintained by either MPP6 or RRP6. However, knowledge regarding the function of MPP6 with respect to in vivo exosome activity remains scarce. Here, we demonstrate a facilitative function of MPP6 that composes a specific part of MTR4-dependent substrate decay by the human exosome. Using RNA polymerase II-transcribed poly(A)+ substrate accumulation as an indicator of a perturbed exosome, we found functional redundancy between RRP6 and MPP6 in the decay of these poly(A)+ transcripts. MTR4 binding to the exosome core via MPP6 was essential for MPP6 to exert its redundancy with RRP6. However, at least for the decay of our identified exosome substrates, MTR4 recruitment by MPP6 was not functionally equivalent to recruitment by RRP6. Genome-wide classification of substrates based on their sensitivity to each exosome component revealed that MPP6 deals with a specific range of substrates and highlights the importance of MTR4 for their decay. Considering recent findings of competitive binding to the exosome between auxiliary complexes, our results suggest that the MPP6-incorporated MTR4-exosome complex is one of the multiple alternative complexes rather than the prevailing one.

Funder

JSPS

Uehara Memorial Foundation

Japan Science Society

Agricultural Technology and Innovation Research Institute

Publisher

Oxford University Press (OUP)

Subject

Genetics

Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3