The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein
Open accessAbstract
HIV-1 Tat activates transcription through binding to human cyclin T1, a regulatory subunit of the TAK/P-TEFb CTD kinase complex. Here we show that the cyclin domain of hCycT1 is necessary and sufficient to interact with Tat and promote cooperative binding to TAR RNA in vitro, as well as mediate Tat transactivation in vivo. A Tat:TAR recognition motif (TRM) was identified at the carboxy-terminal edge of the cyclin domain, and we show that hCycT1 can interact simultaneously with Tat and CDK9 on TAR RNA in vitro. Alanine-scanning mutagenesis of the hCycT1 TRM identified residues that are critical for the interaction with Tat and others that are required specifically for binding of the complex to TAR RNA. Interestingly, we find that the interaction between Tat and hCycT1 requires zinc as well as essential cysteine residues in both proteins. Cloning and characterization of the murine CycT1 protein revealed that it lacks a critical cysteine residue (C261) and forms a weak, zinc-independent complex with HIV-1 Tat that greatly reduces binding to TAR RNA. A point mutation in mCycT1 (Y261C) restores high-affinity, zinc-dependent binding to Tat and TAR in vitro, and rescues Tat transactivation in vivo. Although overexpression of hCycT1 in NIH3T3 cells strongly enhances transcription from an integrated proviral promoter, we find that this fails to overcome all blocks to productive HIV-1 infection in murine cells.
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Cites
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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
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Self-citationCrystal structure of the p27Kip1 cyclin-dependent-kinase inibitor bound to the cyclin A–Cdk2 complex
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Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro
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Self-citationControl of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase
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Cited by
Controlling the elongation phase of transcription with P-TEFb
Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144
Flavopiridol Inactivates P-TEFb and Blocks Most RNA Polymerase II Transcription in Vivo
Chao, S.-H., & Price, D. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102306200 · Cited by 621
Flavopiridol Inhibits P-TEFb and Blocks HIV-1 Replication
Chao, S.-H., Fujinaga, K., Marion, J. E., Taube, R., Sausville, E. A., Senderowicz, A. M., Peterlin, B. M., & Price, D. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000446200 · Cited by 455
Born to run: control of transcription elongation by RNA polymerase II
Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447
Transcriptional and Posttranscriptional Regulation of HIV-1 Gene Expression
Karn, J., & Stoltzfus, C. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006916 · Cited by 437
Metadata
- Authors
- Garber, M. E., Wei, P., KewalRamani, V. N., Mayall, T. P., Herrmann, C. H., Rice, A. P., Littman, D. R., & Jones, K. A.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1998-11-15
- Volume
- 12
- Issue
- 22
- Pages
- 3512-3527
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2135736528
- Cited by
- 431
- References
- 63
- Type
- posted content
- Language
- en
- Open access
- diamond
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- CoChat. (2026). Citation check: The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. https://app.cochat.ai/papers/10.1101/gad.12.22.3512
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- Garber, M. E., Wei, P., KewalRamani, V. N., Mayall, T. P., Herrmann, C. H., Rice, A. P., Littman, D. R., & Jones, K. A. (1998). The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes & Development. https://doi.org/10.1101/gad.12.22.3512
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