Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly | Zendy

Leonid Minakhin | Zendy; Sechal Bhagat | Zendy; Adrian Brunning | Zendy; Elizabeth A. Campbell | Zendy; Seth A. Darst | Zendy; Richard H. Ebright | Zendy; Konstantin Severinov | Zendy

Open Access

Bacterial RNA polymerase subunit ω and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly

Author(s) -

Leonid Minakhin,

Sechal Bhagat,

Adrian Brunning,

Elizabeth A. Campbell,

Seth A. Darst,

Richard H. Ebright,

Konstantin Severinov

Publication year - 2001

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.98.3.892

Subject(s) - rna polymerase , protein subunit , polymerase , biology , specificity factor , rna polymerase i , rna polymerase ii , rna , homologous chromosome , microbiology and biotechnology , dna , biochemistry , gene , promoter , gene expression

Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.

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