Identification of the Specific Interactors of the Human Lariat RNA Debranching Enzyme 1 Protein

International Journal of Molecular Sciences

So Masaki²  Rei Yoshimoto¹  Daisuke Kaida³  Asuka Hata²  Takayuki Satoh³  Mutsuhito Ohno⁴  Naoyuki Kataoka² 

[1] Chemical Genetics Laboratory, RIKEN Advanced Science Institute, Wako, Saitama 351-0198, Japan; E-Mail:;Medical Innovation Center, Laboratory for Malignancy Control Research, Kyoto University Graduate School of Medicine, Sakyo-ku, Kyoto 606-8507, Japan; E-Mails:;Frontier Research Core for Life Sciences, University of Toyama, 2630 Sugitani, Toyama-shi, Toyama 930-0194, Japan; E-Mails:;Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan; E-Mail:

关键词: pre-mRNA splicing;    intron turnover;    RNA lariat;    debranching;    hDbr1;    Xab2;    hDrn1;   

DOI  :  10.3390/ijms16023705

来源: mdpi

【 摘 要 】

In eukaryotes, pre-mRNA splicing is an essential step for gene expression. We have been analyzing post-splicing intron turnover steps in higher eukaryotes. Here, we report protein interaction between human Debranching enzyme 1 (hDbr1) and several factors found in the Intron Large (IL) complex, which is an intermediate complex of the intron degradation pathway. The hDbr1 protein specifically interacts with xeroderma pigmentosum, complementeation group A (XPA)-binding protein 2 (Xab2). We also attempted to identify specific interactors of hDbr1. Co-immunoprecipitation experiments followed by mass spectrometry analysis identified a novel protein as one of the specific interactors of hDbr1. This protein is well conserved among many species and shows the highest similarity to yeast Drn1, so it is designated as human Dbr1 associated ribonuclease 1 (hDrn1). hDrn1 directly interacts with hDbr1 through protein–protein interaction. Furthermore, hDrn1 shuttles between the nucleus and the cytoplasm, as hDbr1 protein does. These findings suggest that hDrn1 has roles in both the nucleus and the cytoplasm, which are highly likely to involve hDbr1.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.