Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

Koh Fujinaga; Ran Taube; Jörg Wimmer; Thomas P. Cujec; B. Matija Peterlin

doi:10.1073/pnas.96.4.1285

Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

Koh Fujinaga, Ran Taube, Jörg Wimmer, Thomas P. Cujec, B. Matija Peterlin

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

124 Scopus citations

Abstract

The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of vital 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.

Original language	English
Pages (from-to)	1285-1290
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	96
Issue number	4
DOIs	https://doi.org/10.1073/pnas.96.4.1285
State	Published - 16 Feb 1999
Externally published	Yes

ASJC Scopus subject areas

General

UN SDGs

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

Access to Document

10.1073/pnas.96.4.1285

Cite this

Fujinaga, K., Taube, R., Wimmer, J., Cujec, T. P., & Peterlin, B. M. (1999). Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. Proceedings of the National Academy of Sciences of the United States of America, 96(4), 1285-1290. https://doi.org/10.1073/pnas.96.4.1285

@article{d6b04bca17c241249839f4b6f3dcfb25,

title = "Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T",

abstract = "The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of vital 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.",

author = "Koh Fujinaga and Ran Taube and J{\"o}rg Wimmer and Cujec, {Thomas P.} and Peterlin, {B. Matija}",

year = "1999",

month = feb,

day = "16",

doi = "10.1073/pnas.96.4.1285",

language = "English",

volume = "96",

pages = "1285--1290",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "4",

}

Fujinaga, K, Taube, R, Wimmer, J, Cujec, TP & Peterlin, BM 1999, 'Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T', Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 4, pp. 1285-1290. https://doi.org/10.1073/pnas.96.4.1285

Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. / Fujinaga, Koh; Taube, Ran; Wimmer, Jörg et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 4, 16.02.1999, p. 1285-1290.

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

TY - JOUR

T1 - Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

AU - Fujinaga, Koh

AU - Taube, Ran

AU - Wimmer, Jörg

AU - Cujec, Thomas P.

AU - Peterlin, B. Matija

PY - 1999/2/16

Y1 - 1999/2/16

N2 - The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of vital 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.

AB - The transcriptional transactivator Tat from HIV binds to the transactivation response element (TAR) RNA to increase rates of elongation of vital 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.

UR - http://www.scopus.com/inward/record.url?scp=0033574077&partnerID=8YFLogxK

U2 - 10.1073/pnas.96.4.1285

DO - 10.1073/pnas.96.4.1285

M3 - Article

C2 - 9990016

AN - SCOPUS:0033574077

SN - 0027-8424

VL - 96

SP - 1285

EP - 1290

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 4

ER -

Interactions between human cyclin T, Tat, and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T

Abstract

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this