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 |
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ASJC Scopus subject areas
- Molecular Biology
- Cancer Research
- Genetics
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A cellular protein which is coprecipitated with HTLV-I rex protein in the presence of the target mRNA. / Katahira, Jun; Siomi, Haruhiko; Ishizaki, Toshimasa; Umemoto, Tomoe; Tanaka, Yuetsu; Shida, Hisatoshi.
In: Oncogene, Vol. 9, No. 12, 12.1994, p. 3535-3544.Research output: Contribution to journal › Article
}
TY - JOUR
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.
UR - http://www.scopus.com/inward/record.url?scp=0028135475&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028135475&partnerID=8YFLogxK
M3 - Article
C2 - 7970714
AN - SCOPUS:0028135475
VL - 9
SP - 3535
EP - 3544
JO - Oncogene
JF - Oncogene
SN - 0950-9232
IS - 12
ER -