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Structural basis of transcription initiation.

ABSTRACT: During transcription initiation, RNA polymerase (RNAP) binds and unwinds promoter DNA to form an RNAP-promoter open complex. We have determined crystal structures at 2.9 and 3.0 Å resolution of functional transcription initiation complexes comprising Thermus thermophilus RNA polymerase, ?(A), and a promoter DNA fragment corresponding to the transcription bubble and downstream double-stranded DNA of the RNAP-promoter open complex. The structures show that ? recognizes the -10 element and discriminator element through interactions that include the unstacking and insertion into pockets of three DNA bases and that RNAP recognizes the -4/+2 region through interactions that include the unstacking and insertion into a pocket of the +2 base. The structures further show that interactions between ? and template-strand single-stranded DNA (ssDNA) preorganize template-strand ssDNA to engage the RNAP active center.

SUBMITTER: Zhang Y

PROVIDER: S-EPMC3593053 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

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Structural basis of transcription initiation.

Zhang Yu Y Feng Yu Y Chatterjee Sujoy S Tuske Steve S Ho Mary X MX Arnold Eddy E Ebright Richard H RH

Science (New York, N.Y.) 20121018 6110

During transcription initiation, RNA polymerase (RNAP) binds and unwinds promoter DNA to form an RNAP-promoter open complex. We have determined crystal structures at 2.9 and 3.0 Å resolution of functional transcription initiation complexes comprising Thermus thermophilus RNA polymerase, σ(A), and a promoter DNA fragment corresponding to the transcription bubble and downstream double-stranded DNA of the RNAP-promoter open complex. The structures show that σ recognizes the -10 element and discrimi ...[more]

PMID: 23086998

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