Fibrillarin binds to a 3′ cis-regulatory element in pre-mRNA of uvi15+ in fission yeast

Yeun Kyu Jang; Minkyu Kim; Sang Dai Park

doi:10.1016/S0006-291X(02)00611-3

Fibrillarin binds to a 3′ cis-regulatory element in pre-mRNA of uvi15⁺ in fission yeast

Yeun Kyu Jang, Minkyu Kim, Sang Dai Park

Department of Systems Biology

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

3 Citations (Scopus)

Abstract

uvi15⁺ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15⁺ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.

Original language	English
Pages (from-to)	1184-1190
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	294
Issue number	5
DOIs	https://doi.org/10.1016/S0006-291X(02)00611-3
Publication status	Published - 2002

Bibliographical note

Funding Information:
We thank Drs. Marvin Wickens and M. Yamamoto for providing yeast strains and plasmids used in three-hybrid assay and S. pombe cell strain, respectively. We also thank Dr. O. Hwang for critical reading of the manuscript. This work was supported in part by a grant for the leading scientists from the Korea Science and Engineering Foundation (2001) to S.D. Park., M.K., and S.D.P. are supported by a BK21 Research Fellowship from the Korea Ministry of Education.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/S0006-291X(02)00611-3

Cite this

@article{fd50699755784652b7dcdec1d20bcc73,

title = "Fibrillarin binds to a 3′ cis-regulatory element in pre-mRNA of uvi15+ in fission yeast",

abstract = "uvi15+ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15+ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.",

author = "Jang, {Yeun Kyu} and Minkyu Kim and Park, {Sang Dai}",

note = "Funding Information: We thank Drs. Marvin Wickens and M. Yamamoto for providing yeast strains and plasmids used in three-hybrid assay and S. pombe cell strain, respectively. We also thank Dr. O. Hwang for critical reading of the manuscript. This work was supported in part by a grant for the leading scientists from the Korea Science and Engineering Foundation (2001) to S.D. Park., M.K., and S.D.P. are supported by a BK21 Research Fellowship from the Korea Ministry of Education.",

year = "2002",

doi = "10.1016/S0006-291X(02)00611-3",

language = "English",

volume = "294",

pages = "1184--1190",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "5",

}

TY - JOUR

T1 - Fibrillarin binds to a 3′ cis-regulatory element in pre-mRNA of uvi15+ in fission yeast

AU - Jang, Yeun Kyu

AU - Kim, Minkyu

AU - Park, Sang Dai

N1 - Funding Information: We thank Drs. Marvin Wickens and M. Yamamoto for providing yeast strains and plasmids used in three-hybrid assay and S. pombe cell strain, respectively. We also thank Dr. O. Hwang for critical reading of the manuscript. This work was supported in part by a grant for the leading scientists from the Korea Science and Engineering Foundation (2001) to S.D. Park., M.K., and S.D.P. are supported by a BK21 Research Fellowship from the Korea Ministry of Education.

PY - 2002

Y1 - 2002

N2 - uvi15+ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15+ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.

AB - uvi15+ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15+ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.

UR - http://www.scopus.com/inward/record.url?scp=0036290028&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036290028&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(02)00611-3

DO - 10.1016/S0006-291X(02)00611-3

M3 - Article

C2 - 12074602

AN - SCOPUS:0036290028

SN - 0006-291X

VL - 294

SP - 1184

EP - 1190

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 5

ER -