TY - JOUR
T1 - Canine cyclin T1 rescues equine infectious anemia virus tat trans- activation in human cells
AU - Albrecht, Todd R.
AU - Lund, Lars H.
AU - Garcia-Blanco, Mariano A.
N1 - Funding Information:
We thank Bryan R. Cullen and Paul Bieniasz for sharing of data and reagents before publication. We also thank B. M. Peterlin for sharing data before publication. We thank members of the Garcia-Blanco laboratory, most especially Carles Suñe and Aaron Goldstrohm for advice and critical reading of the manuscript. We are grateful to Katherine Jones, Bryan R. Cullen, Britta Wahren, and David Derse for plasmids and other valuable reagents. This work was supported by a grant from the NIH to M.A.G-B and by funds provided by the Center for AIDS Research at Duke University Medical Center. LHL was supported by a Howard Hughes Medical Institute Fellowship for Medical Students.
PY - 2000/3/1
Y1 - 2000/3/1
N2 - Human immunodeficiency virus-1 Tat protein and human Cyclin T1 mediate transcriptional activation by enhancing the elongation efficiency of RNA polymerase II. Activation of transcription of the related equine infectious anemia virus (EIAV) requires a similar protein known as eTat, which does not function in human cells. Expression of equine Cyclin T1 in human cells rescues eTat function, suggesting a general mechanism of transcription activation among lentiviruses. Here we present the cloning of Cyclin T1 from canine D17 osteosarcoma cells, which support EIAV transactivation, and show that canine Cyclin T1 confers eTat transactivation to human cells. A two- amino-acid change, from 79-proline-glycine-80 to 79-histidine-arginine-80, confers on the human Cyclin T1 the ability to cooperate with eTat in transcriptional activation. These findings suggested that the regions of Cyclin T1 that interact with lentiviral Tat proteins and TAR RNA elements form an extended domain, which very likely has a conserved fold. (C) 2000 Academic Press.
AB - Human immunodeficiency virus-1 Tat protein and human Cyclin T1 mediate transcriptional activation by enhancing the elongation efficiency of RNA polymerase II. Activation of transcription of the related equine infectious anemia virus (EIAV) requires a similar protein known as eTat, which does not function in human cells. Expression of equine Cyclin T1 in human cells rescues eTat function, suggesting a general mechanism of transcription activation among lentiviruses. Here we present the cloning of Cyclin T1 from canine D17 osteosarcoma cells, which support EIAV transactivation, and show that canine Cyclin T1 confers eTat transactivation to human cells. A two- amino-acid change, from 79-proline-glycine-80 to 79-histidine-arginine-80, confers on the human Cyclin T1 the ability to cooperate with eTat in transcriptional activation. These findings suggested that the regions of Cyclin T1 that interact with lentiviral Tat proteins and TAR RNA elements form an extended domain, which very likely has a conserved fold. (C) 2000 Academic Press.
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U2 - 10.1006/viro.1999.0141
DO - 10.1006/viro.1999.0141
M3 - Article
C2 - 10683321
AN - SCOPUS:0034009884
SN - 0042-6822
VL - 268
SP - 7
EP - 11
JO - Virology
JF - Virology
IS - 1
ER -