Protein family review - The sigma(70) family of sigma factors

Paget, Mark and Helmann, John (2003) Protein family review - The sigma(70) family of sigma factors. Genome Biology, 4 (1). ISSN 1465-6906

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Abstract

Members of the sigma(70) family of sigma factors are components of the RNA polymerase holoenzyme that direct bacterial or plastid core RNA polymerase to specific promoter elements that are situated 10 and 35 base-pairs upstream of transcription-initiation points. Members of the sigma(70) family also function as contact points for some activator proteins, such as PhoB and lambdacl, and play a role in the initiation process itself. The primary sigma factor, which is essential for general transcription in exponentially growing cells, is reversibly associated with RNA polymerase and can be replaced by alternative factors that co-ordinately express genes involved in diverse functions, such as stress responses, morphological development and iron uptake. On the basis of gene structure and function, members of the sigma(70) family can broadly be divided into four main groups. Sequence alignments of the sigma(70) family members reveal that they have four conserved regions, although the highest conservation is found in regions 2 and 4, which are involved in binding to RNA polymerase, recognizing promoters and separating DNA strands (so-called 'DNA melting'). The division of the linear sequence of sigma(70) factors into four regions is largely supported by recent structural data indicating that primary sigma factors have three stable domains that incorporate regions 2, 3 and 4. Furthermore, structures of the RNA polymerase holoenzyme have revealed that these domains of sigma(70) are spread out across one face of RNA polymerase. These structural data are starting to illuminate the mechanistic role of factors in transcription initiation.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Mark Paget
Date Deposited: 06 Feb 2012 21:08
Last Modified: 17 Jul 2012 08:30
URI: http://sro.sussex.ac.uk/id/eprint/29716
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