Abstract
The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of viral transcription. Human cyclin T supports these interactions between Tat and TAR. In this study, we report the sequence of mouse cyclin T and identify the residues from positions 1 to 281 in human cyclin T that bind to Tat and TAR. Mouse cyclin T binds to Tat weakly and is unable to facilitate interactions between Tat and TAR. Reciprocal exchanges of the cysteine and tyrosine at position 261 in human and mouse cyclin T proteins also render human cyclin T inactive and mouse cyclin T active. These findings reveal the molecular basis for the restriction of Tat transactivation in rodent cells.
MeSH Terms
Amino Acid Sequence
Amino Acid Substitution
Animals
CHO Cells
Chloramphenicol O-Acetyltransferase/metabolism
Cricetinae
Cyclin T
Cyclins/chemistry,genetics,metabolism
Cysteine
Gene Products, tat/metabolism
HIV Long Terminal Repeat/physiology
Humans
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
Recombinant Fusion Proteins/metabolism
Recombinant Proteins/chemistry,metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Tyrosine
Chemicals
CCNT1 protein, human
Ccnt1 protein, mouse
Cyclin T
Cyclins
Gene Products, tat
Recombinant Fusion Proteins
Recombinant Proteins
Tyrosine
Chloramphenicol O-Acetyltransferase
Cysteine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Fujinaga K
Howard Hughes Medical Institute, Departments of Medicine, Microbiology, and Immunology, University of California, San Francisco, CA 94143-0703, USA.
Taube R
Wimmer J
Cujec T P
Peterlin B M
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