hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA

Dong Hyoung Lee; Mi Hyun Lim; Dong Ye Youn; Seung Eun Jung; Young Soo Ahn; Yoshihide Tsujimoto; Jeong Hwa Lee

doi:10.1016/j.bbrc.2009.03.069

hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA

Dong Hyoung Lee, Mi Hyun Lim, Dong Ye Youn, Seung Eun Jung, Young Soo Ahn, Yoshihide Tsujimoto, Jeong Hwa Lee

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

26 Scopus citations

Abstract

We previously reported that the CA-repeat sequence in the 3′-untranslated region (3′UTR) of bcl-2 mRNA is involved in the decay of bcl-2 mRNA. However, the trans-acting factor for the CA element in bcl-2 mRNA remains unidentified. The heterogeneous nuclear ribonucleoprotein L (hnRNP L), an intron splicing factor, has been reported to bind to CA repeats and CA clusters in the 3′UTR of several genes. We reported herein that the CA repeats of bcl-2 mRNA have the potential to form a distinct ribonuclear protein complex in cytoplasmic extracts of MCF-7 cells, as evidenced by RNA electrophoretic mobility shift assays (REMSA). A super-shift assay using the hnRNP L antibody completely shifted the complex. Immunoprecipitation with the hnRNP L antibody and MCF-7 cells followed by RT-PCR revealed that hnRNP L interacts with endogenous bcl-2 mRNA in vivo. Furthermore, the suppression of hnRNP L in MCF-7 cells by the transfection of siRNA for hnRNP L resulted in a delay in the degradation of RNA transcripts including CA repeats of bcl-2 mRNA in vitro, suggesting that the interaction between hnRNPL and CA repeats of bcl-2 mRNA participates in destabilizing bcl-2 mRNA.

Original language	English
Pages (from-to)	583-587
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	382
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2009.03.069
State	Published - 8 May 2009

Bibliographical note

Funding Information:
This work was supported by the Korea Science and Engineering Foundation (KOSEF) grant funded by the Korean government (MOST) (No. R01-2006-000-10208-0) and a grant from Solution-Oriented Research for Science and Technology, Japan Science and Technology Agency to YT.

Keywords

CA repeats
bcl-2
hnRNP L
mRNA stability

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10.1016/j.bbrc.2009.03.069

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title = "hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA",

abstract = "We previously reported that the CA-repeat sequence in the 3′-untranslated region (3′UTR) of bcl-2 mRNA is involved in the decay of bcl-2 mRNA. However, the trans-acting factor for the CA element in bcl-2 mRNA remains unidentified. The heterogeneous nuclear ribonucleoprotein L (hnRNP L), an intron splicing factor, has been reported to bind to CA repeats and CA clusters in the 3′UTR of several genes. We reported herein that the CA repeats of bcl-2 mRNA have the potential to form a distinct ribonuclear protein complex in cytoplasmic extracts of MCF-7 cells, as evidenced by RNA electrophoretic mobility shift assays (REMSA). A super-shift assay using the hnRNP L antibody completely shifted the complex. Immunoprecipitation with the hnRNP L antibody and MCF-7 cells followed by RT-PCR revealed that hnRNP L interacts with endogenous bcl-2 mRNA in vivo. Furthermore, the suppression of hnRNP L in MCF-7 cells by the transfection of siRNA for hnRNP L resulted in a delay in the degradation of RNA transcripts including CA repeats of bcl-2 mRNA in vitro, suggesting that the interaction between hnRNPL and CA repeats of bcl-2 mRNA participates in destabilizing bcl-2 mRNA.",

keywords = "CA repeats, bcl-2, hnRNP L, mRNA stability",

author = "Lee, {Dong Hyoung} and Lim, {Mi Hyun} and Youn, {Dong Ye} and Jung, {Seung Eun} and Ahn, {Young Soo} and Yoshihide Tsujimoto and Lee, {Jeong Hwa}",

note = "Funding Information: This work was supported by the Korea Science and Engineering Foundation (KOSEF) grant funded by the Korean government (MOST) (No. R01-2006-000-10208-0) and a grant from Solution-Oriented Research for Science and Technology, Japan Science and Technology Agency to YT.",

year = "2009",

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doi = "10.1016/j.bbrc.2009.03.069",

language = "English",

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T1 - hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA

AU - Lee, Dong Hyoung

AU - Lim, Mi Hyun

AU - Youn, Dong Ye

AU - Jung, Seung Eun

AU - Ahn, Young Soo

AU - Tsujimoto, Yoshihide

AU - Lee, Jeong Hwa

N1 - Funding Information: This work was supported by the Korea Science and Engineering Foundation (KOSEF) grant funded by the Korean government (MOST) (No. R01-2006-000-10208-0) and a grant from Solution-Oriented Research for Science and Technology, Japan Science and Technology Agency to YT.

PY - 2009/5/8

Y1 - 2009/5/8

N2 - We previously reported that the CA-repeat sequence in the 3′-untranslated region (3′UTR) of bcl-2 mRNA is involved in the decay of bcl-2 mRNA. However, the trans-acting factor for the CA element in bcl-2 mRNA remains unidentified. The heterogeneous nuclear ribonucleoprotein L (hnRNP L), an intron splicing factor, has been reported to bind to CA repeats and CA clusters in the 3′UTR of several genes. We reported herein that the CA repeats of bcl-2 mRNA have the potential to form a distinct ribonuclear protein complex in cytoplasmic extracts of MCF-7 cells, as evidenced by RNA electrophoretic mobility shift assays (REMSA). A super-shift assay using the hnRNP L antibody completely shifted the complex. Immunoprecipitation with the hnRNP L antibody and MCF-7 cells followed by RT-PCR revealed that hnRNP L interacts with endogenous bcl-2 mRNA in vivo. Furthermore, the suppression of hnRNP L in MCF-7 cells by the transfection of siRNA for hnRNP L resulted in a delay in the degradation of RNA transcripts including CA repeats of bcl-2 mRNA in vitro, suggesting that the interaction between hnRNPL and CA repeats of bcl-2 mRNA participates in destabilizing bcl-2 mRNA.

AB - We previously reported that the CA-repeat sequence in the 3′-untranslated region (3′UTR) of bcl-2 mRNA is involved in the decay of bcl-2 mRNA. However, the trans-acting factor for the CA element in bcl-2 mRNA remains unidentified. The heterogeneous nuclear ribonucleoprotein L (hnRNP L), an intron splicing factor, has been reported to bind to CA repeats and CA clusters in the 3′UTR of several genes. We reported herein that the CA repeats of bcl-2 mRNA have the potential to form a distinct ribonuclear protein complex in cytoplasmic extracts of MCF-7 cells, as evidenced by RNA electrophoretic mobility shift assays (REMSA). A super-shift assay using the hnRNP L antibody completely shifted the complex. Immunoprecipitation with the hnRNP L antibody and MCF-7 cells followed by RT-PCR revealed that hnRNP L interacts with endogenous bcl-2 mRNA in vivo. Furthermore, the suppression of hnRNP L in MCF-7 cells by the transfection of siRNA for hnRNP L resulted in a delay in the degradation of RNA transcripts including CA repeats of bcl-2 mRNA in vitro, suggesting that the interaction between hnRNPL and CA repeats of bcl-2 mRNA participates in destabilizing bcl-2 mRNA.

KW - CA repeats

KW - bcl-2

KW - hnRNP L

KW - mRNA stability

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JO - Biochemical and Biophysical Research Communications

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ER -

hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA

Abstract

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Keywords

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