An Arabidopsis splicing RNP variant STEP1 regulates telomere length homeostasis by restricting access of nuclease and telomerase

Hyun Hee Yoo; Chian Kwon; In Kwon Chung

doi:10.1007/s10059-010-0115-y

An Arabidopsis splicing RNP variant STEP1 regulates telomere length homeostasis by restricting access of nuclease and telomerase

Hyun Hee Yoo, Chian Kwon, In Kwon Chung

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Telomere is an essential DNA-protein complex composed of repetitive DNA and binding proteins to protect the chromosomal ends in eukaryotes. Telomere length is regulated by a specialized RNA-dependent DNA polymerase, telomerase and associated proteins. We show here a potential role of STEP1 that was previously isolated by affinity chromatography in controlling telomere length. While STEP1 requires both RNA-binding domains for telomere binding and subsequent DNA protection, it requires only one RBD to interact with telomerase. The differential telomerase inhibitory activity depending on STEP1 concentrations may suggest that STEP1 contributes to controlling telomere length homeostasis, likely by limiting the accessibility of nuclease or telomerase to telomeric DNA.

Original language	English
Pages (from-to)	279-283
Number of pages	5
Journal	Molecules and cells
Volume	30
Issue number	3
DOIs	https://doi.org/10.1007/s10059-010-0115-y
Publication status	Published - 2010 Sept

Bibliographical note

Funding Information:
This work was supported by grants from the Korea Research Foundation [M1075604000107N560400110] and the Korean Ministry of Education, Science, and Technology through the WCU project [R31-2008-000-10086-0].

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1007/s10059-010-0115-y

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title = "An Arabidopsis splicing RNP variant STEP1 regulates telomere length homeostasis by restricting access of nuclease and telomerase",

abstract = "Telomere is an essential DNA-protein complex composed of repetitive DNA and binding proteins to protect the chromosomal ends in eukaryotes. Telomere length is regulated by a specialized RNA-dependent DNA polymerase, telomerase and associated proteins. We show here a potential role of STEP1 that was previously isolated by affinity chromatography in controlling telomere length. While STEP1 requires both RNA-binding domains for telomere binding and subsequent DNA protection, it requires only one RBD to interact with telomerase. The differential telomerase inhibitory activity depending on STEP1 concentrations may suggest that STEP1 contributes to controlling telomere length homeostasis, likely by limiting the accessibility of nuclease or telomerase to telomeric DNA.",

author = "Yoo, {Hyun Hee} and Chian Kwon and Chung, {In Kwon}",

note = "Funding Information: This work was supported by grants from the Korea Research Foundation [M1075604000107N560400110] and the Korean Ministry of Education, Science, and Technology through the WCU project [R31-2008-000-10086-0].",

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doi = "10.1007/s10059-010-0115-y",

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AU - Yoo, Hyun Hee

AU - Kwon, Chian

AU - Chung, In Kwon

N1 - Funding Information: This work was supported by grants from the Korea Research Foundation [M1075604000107N560400110] and the Korean Ministry of Education, Science, and Technology through the WCU project [R31-2008-000-10086-0].

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N2 - Telomere is an essential DNA-protein complex composed of repetitive DNA and binding proteins to protect the chromosomal ends in eukaryotes. Telomere length is regulated by a specialized RNA-dependent DNA polymerase, telomerase and associated proteins. We show here a potential role of STEP1 that was previously isolated by affinity chromatography in controlling telomere length. While STEP1 requires both RNA-binding domains for telomere binding and subsequent DNA protection, it requires only one RBD to interact with telomerase. The differential telomerase inhibitory activity depending on STEP1 concentrations may suggest that STEP1 contributes to controlling telomere length homeostasis, likely by limiting the accessibility of nuclease or telomerase to telomeric DNA.

AB - Telomere is an essential DNA-protein complex composed of repetitive DNA and binding proteins to protect the chromosomal ends in eukaryotes. Telomere length is regulated by a specialized RNA-dependent DNA polymerase, telomerase and associated proteins. We show here a potential role of STEP1 that was previously isolated by affinity chromatography in controlling telomere length. While STEP1 requires both RNA-binding domains for telomere binding and subsequent DNA protection, it requires only one RBD to interact with telomerase. The differential telomerase inhibitory activity depending on STEP1 concentrations may suggest that STEP1 contributes to controlling telomere length homeostasis, likely by limiting the accessibility of nuclease or telomerase to telomeric DNA.

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An Arabidopsis splicing RNP variant STEP1 regulates telomere length homeostasis by restricting access of nuclease and telomerase

Abstract

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