Multiple hTAF(II)31-binding motifs in the intrinsically unfolded transcriptional activation domain of VP16.
Transcriptional activation domain (TAD) in virion protein 16 (VP16) of herpes simplex virus does not have any globular structure, yet exhibits a potent transcriptional activity. In order to probe the structural basis for the transcriptional activity of VP16 TAD, we have used NMR spectroscopy to investigate its detailed structural features. Results show that an unbound VP16 TAD is not merely "unstructured" but contains four short motifs (residues 424-433, 442-446, 465-467 and 472-479) with transient structural order. Pre-structured motifs in other intrinsically unfolded proteins (IUPs) were shown to be critically involved in target protein binding. The 472-479 motif was previously shown to bind to hTAF(II)31, whereas the hTAF(II)31-binding ability of other motifs found in this study has not been addressed. The VP16 TAD represents another IUP whose prestructured motifs mediate promiscuous binding to various target proteins.
Kim
Do-Hyoung
DH
Bioinformatics Research Center, KRIBB, Daejeon 305-806, Korea.
Lee
Si-Hyung
SH
Nam
Ki Hoon
KH
Chi
Seung-Wook
SW
Chang
Iksoo
I
Han
Kyou-Hoon
KH
D020816:Amino Acid Motifs; D001665:Binding Sites; D017405:Herpes Simplex Virus Protein Vmw65 / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D035381:TATA-Binding Protein Associated Factors / Q000378:metabolism*; D035362:Transcription Factor TFIID / Q000378:metabolism*; D015533:Transcriptional Activation / Q000502:physiology
D017405:Herpes Simplex Virus Protein Vmw65; D011994:Recombinant Proteins; C106849:TAF9 protein, human; D035381:TATA-Binding Protein Associated Factors; D035362:Transcription Factor TFIID