A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA

Jun Katahira; Haruhiko Siomi; Toshimasa Ishizaki; Tomoe Umemoto; Yuetsu Tanaka; Hisatoshi Shida

A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA

Jun Katahira, Haruhiko Siomi, Toshimasa Ishizaki, Tomoe Umemoto, Yuetsu Tanaka, Hisatoshi Shida

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

Abstract

We examined the cellular protein(s) which can associate with Rex protein of human T cell leukemia virus type I (HTLV-I), using Rex-maltose binding protein (MBP) fusion protein. Immunoprecipitation of RexMBP with anti-MBP antibody revealed that a 24 kD protein (p24) associated with RexMBP only in the presence of Rex-responsive mRNA, The fact that p24 was present in both the nucleus and the cytoplasm is consistent with a role of Rex in the nucleo-cytoplasmic transport of viral mRNAs. P24 did not interact with nonfunctional Rex mutant proteins even if they had RNA binding activity in vitro. These results suggest the possible involvement of p24 in the Rex function through a complex formation with Rex on Rex-responsive mRNA.

Original language	English
Pages (from-to)	3535-3544
Number of pages	10
Journal	Oncogene
Volume	9
Issue number	12
Publication status	Published - 1994 Dec
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Genetics
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

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title = "A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA",

abstract = "We examined the cellular protein(s) which can associate with Rex protein of human T cell leukemia virus type I (HTLV-I), using Rex-maltose binding protein (MBP) fusion protein. Immunoprecipitation of RexMBP with anti-MBP antibody revealed that a 24 kD protein (p24) associated with RexMBP only in the presence of Rex-responsive mRNA, The fact that p24 was present in both the nucleus and the cytoplasm is consistent with a role of Rex in the nucleo-cytoplasmic transport of viral mRNAs. P24 did not interact with nonfunctional Rex mutant proteins even if they had RNA binding activity in vitro. These results suggest the possible involvement of p24 in the Rex function through a complex formation with Rex on Rex-responsive mRNA.",

author = "Jun Katahira and Haruhiko Siomi and Toshimasa Ishizaki and Tomoe Umemoto and Yuetsu Tanaka and Hisatoshi Shida",

year = "1994",

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T1 - A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA

AU - Katahira, Jun

AU - Siomi, Haruhiko

AU - Ishizaki, Toshimasa

AU - Umemoto, Tomoe

AU - Tanaka, Yuetsu

AU - Shida, Hisatoshi

PY - 1994/12

Y1 - 1994/12

N2 - We examined the cellular protein(s) which can associate with Rex protein of human T cell leukemia virus type I (HTLV-I), using Rex-maltose binding protein (MBP) fusion protein. Immunoprecipitation of RexMBP with anti-MBP antibody revealed that a 24 kD protein (p24) associated with RexMBP only in the presence of Rex-responsive mRNA, The fact that p24 was present in both the nucleus and the cytoplasm is consistent with a role of Rex in the nucleo-cytoplasmic transport of viral mRNAs. P24 did not interact with nonfunctional Rex mutant proteins even if they had RNA binding activity in vitro. These results suggest the possible involvement of p24 in the Rex function through a complex formation with Rex on Rex-responsive mRNA.

AB - We examined the cellular protein(s) which can associate with Rex protein of human T cell leukemia virus type I (HTLV-I), using Rex-maltose binding protein (MBP) fusion protein. Immunoprecipitation of RexMBP with anti-MBP antibody revealed that a 24 kD protein (p24) associated with RexMBP only in the presence of Rex-responsive mRNA, The fact that p24 was present in both the nucleus and the cytoplasm is consistent with a role of Rex in the nucleo-cytoplasmic transport of viral mRNAs. P24 did not interact with nonfunctional Rex mutant proteins even if they had RNA binding activity in vitro. These results suggest the possible involvement of p24 in the Rex function through a complex formation with Rex on Rex-responsive mRNA.

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A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA

Abstract

ASJC Scopus subject areas

UN SDGs

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