The transcriptional factor Osterix directly interacts with RNA helicase A

Bruna Rabelo Amorim; Hirohiko Okamura; Kaya Yoshida; Lihong Qiu; Hiroyuki Morimoto; Tatsuji Haneji

doi:10.1016/j.bbrc.2007.01.150

The transcriptional factor Osterix directly interacts with RNA helicase A

Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida, Lihong Qiu, Hiroyuki Morimoto, Tatsuji Haneji

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

12 Citations (Scopus)

Abstract

Osterix is an osteoblast-specific transcriptional factor, required for bone formation and osteoblast differentiation. Here, we identified new Osterix interacting factors by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Among the candidates, RNA helicase A was identified to interact with Osterix. To determine the interaction of Osterix with RNA helicase A, immunoprecipitation assay was performed. Western analysis confirmed the association between Osterix and RNA helicase A. Immunocytochemical analysis also showed that Osterix and RNA helicase A were co-localized in HEK 293 cells. Our data suggest that RNA helicase A might be a component of Osterix regulation.

Original language	English
Pages (from-to)	347-351
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	355
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2007.01.150
Publication status	Published - Apr 6 2007
Externally published	Yes

Keywords

MALDI-TOF
Osterix
RNA helicase A

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2007.01.150

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title = "The transcriptional factor Osterix directly interacts with RNA helicase A",

abstract = "Osterix is an osteoblast-specific transcriptional factor, required for bone formation and osteoblast differentiation. Here, we identified new Osterix interacting factors by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Among the candidates, RNA helicase A was identified to interact with Osterix. To determine the interaction of Osterix with RNA helicase A, immunoprecipitation assay was performed. Western analysis confirmed the association between Osterix and RNA helicase A. Immunocytochemical analysis also showed that Osterix and RNA helicase A were co-localized in HEK 293 cells. Our data suggest that RNA helicase A might be a component of Osterix regulation.",

keywords = "MALDI-TOF, Osterix, RNA helicase A",

author = "Amorim, {Bruna Rabelo} and Hirohiko Okamura and Kaya Yoshida and Lihong Qiu and Hiroyuki Morimoto and Tatsuji Haneji",

note = "Funding Information: We thank Dr. T. Iwata for help on the analysis of MALDI-TOF mass spectrometry and valuable discussion. We also thank Mrs. E. Sasaki for her skilful technical assistance. This study was supported in part by grants from the Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan.",

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doi = "10.1016/j.bbrc.2007.01.150",

language = "English",

volume = "355",

pages = "347--351",

journal = "Biochemical and Biophysical Research Communications",

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T1 - The transcriptional factor Osterix directly interacts with RNA helicase A

AU - Amorim, Bruna Rabelo

AU - Okamura, Hirohiko

AU - Yoshida, Kaya

AU - Qiu, Lihong

AU - Morimoto, Hiroyuki

AU - Haneji, Tatsuji

N1 - Funding Information: We thank Dr. T. Iwata for help on the analysis of MALDI-TOF mass spectrometry and valuable discussion. We also thank Mrs. E. Sasaki for her skilful technical assistance. This study was supported in part by grants from the Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan.

PY - 2007/4/6

Y1 - 2007/4/6

N2 - Osterix is an osteoblast-specific transcriptional factor, required for bone formation and osteoblast differentiation. Here, we identified new Osterix interacting factors by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Among the candidates, RNA helicase A was identified to interact with Osterix. To determine the interaction of Osterix with RNA helicase A, immunoprecipitation assay was performed. Western analysis confirmed the association between Osterix and RNA helicase A. Immunocytochemical analysis also showed that Osterix and RNA helicase A were co-localized in HEK 293 cells. Our data suggest that RNA helicase A might be a component of Osterix regulation.

AB - Osterix is an osteoblast-specific transcriptional factor, required for bone formation and osteoblast differentiation. Here, we identified new Osterix interacting factors by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Among the candidates, RNA helicase A was identified to interact with Osterix. To determine the interaction of Osterix with RNA helicase A, immunoprecipitation assay was performed. Western analysis confirmed the association between Osterix and RNA helicase A. Immunocytochemical analysis also showed that Osterix and RNA helicase A were co-localized in HEK 293 cells. Our data suggest that RNA helicase A might be a component of Osterix regulation.

KW - MALDI-TOF

KW - Osterix

KW - RNA helicase A

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

The transcriptional factor Osterix directly interacts with RNA helicase A

Abstract

Keywords

ASJC Scopus subject areas

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