Abstract
Archaea possess a basal transcriptional apparatus that resembles that of eukaryotes. Here we report the 2.1-A crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts. However, in comparison with the eukaryotic complexes, the archaeal TBP-DNA interface is more symmetrical, and in this structure the orientation of the preinitiation complex assembly on the promoter is inverted with respect to that seen in all crystal structures of comparable eukaryotic systems. This study of the structural details of an archaeal transcription factor complex presents the opportunity to examine the evolution of the basal eukaryotic transcriptional apparatus from a stereochemical viewpoint and to extend our understanding of the physical biochemistry of transcriptional initiation.
MeSH Terms
Amino Acid Sequence
Arabidopsis
Archaea/metabolism
Base Sequence
Computer Graphics
Crystallography, X-Ray
DNA/chemistry,metabolism
DNA-Binding Proteins/biosynthesis,chemistry,metabolism
Humans
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
Oligodeoxyribonucleotides/chemistry,metabolism
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins/biosynthesis,chemistry
Sequence Deletion
Species Specificity
TATA Box
TATA-Box Binding Protein
Transcription Factor TFIIB
Transcription Factors/biosynthesis,chemistry,metabolism
Chemicals
DNA-Binding Proteins
Oligodeoxyribonucleotides
Recombinant Proteins
TATA-Box Binding Protein
Transcription Factor TFIIB
Transcription Factors
DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kosa P F
Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, JWG 423, New Haven CT 06511, USA.
Ghosh G
DeDecker B S
Sigler P B
References (25)
25 references, click to expand
-
In vivo definition of an archaeal promoter.
J Bacteriol. 1995 Apr;177(7):1844-9
PMID: 7896710
-
Elements of an archaeal promoter defined by mutational analysis.
Nucleic Acids Res. 1992 Oct 25;20(20):5423-8
PMID: 1279520
-
Enzymes and proteins from organisms that grow near and above 100 degrees C.
Annu Rev Microbiol. 1993;47:627-58
PMID: 8257111
-
Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II.
Genes Dev. 1993 Jun;7(6):1021-32
PMID: 8504927
-
Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons.
Proteins. 1991;11(4):281-96
PMID: 1758883
-
Crystal structure of a TFIIB-TBP-TATA-element ternary complex.
Nature. 1995 Sep 14;377(6545):119-28
PMID: 7675079
-
Complete nucleotide sequence of an archaeal (Pyrococcus woesei) gene encoding a homolog of eukaryotic transcription factor IIB (TFIIB).
Nucleic Acids Res. 1993 Jun 25;21(12):2942
PMID: 8332505
-
Crystal structure of a yeast TFIIA/TBP/DNA complex.
Nature. 1996 May 9;381(6578):127-51
PMID: 8610010
-
Improved methods for building protein models in electron density maps and the location of errors in these models.
Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9
PMID: 2025413
-
Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein.
Cell. 1995 Sep 8;82(5):857-67
PMID: 7671313
-
The crystal structure of a hyperthermophilic archaeal TATA-box binding protein.
J Mol Biol. 1996 Dec 20;264(5):1072-84
PMID: 9000631
-
Crystal structure of a human TATA box-binding protein/TATA element complex.
Proc Natl Acad Sci U S A. 1996 May 14;93(10):4862-7
PMID: 8643494
-
Molecular cloning of the transcription factor TFIIB homolog from Sulfolobus shibatae.
Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):6077-81
PMID: 7597084
-
The TATA-binding protein: a general transcription factor in eukaryotes and archaebacteria.
Science. 1994 May 27;264(5163):1326-9
PMID: 8191287
-
How proteins recognize the TATA box.
J Mol Biol. 1996 Aug 16;261(2):239-54
PMID: 8757291
-
Two transcription factors related with the eucaryal transcription factors TATA-binding protein and transcription factor IIB direct promoter recognition by an archaeal RNA polymerase.
J Biol Chem. 1996 Nov 22;271(47):30144-8
PMID: 8939964
-
Transcription in archaea: similarity to that in eucarya.
Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):5768-72
PMID: 7597027
-
1.9 A resolution refined structure of TBP recognizing the minor groove of TATAAAAG.
Nat Struct Biol. 1994 Sep;1(9):638-53
PMID: 7634103
-
Crystal structure of the yeast TFIIA/TBP/DNA complex.
Science. 1996 May 10;272(5263):830-6
PMID: 8629014
-
The CCP4 suite: programs for protein crystallography.
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3
PMID: 15299374
-
Cloning and functional analysis of the TATA binding protein from Sulfolobus shibatae.
Nucleic Acids Res. 1995 May 25;23(10):1775-81
PMID: 7784182
-
Crystal structure of a yeast TBP/TATA-box complex.
Nature. 1993 Oct 7;365(6446):512-20
PMID: 8413604
-
Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.
J Mol Biol. 1994 Oct 14;243(1):100-15
PMID: 7932732
-
Transcription factor IID in the Archaea: sequences in the Thermococcus celer genome would encode a product closely related to the TATA-binding protein of eukaryotes.
Proc Natl Acad Sci U S A. 1994 May 10;91(10):4180-4
PMID: 8183889
-
Co-crystal structure of TBP recognizing the minor groove of a TATA element.
Nature. 1993 Oct 7;365(6446):520-7
PMID: 8413605