This careful control of metalloprotein assembly may well be

This careful control of metalloprotein assembly may well be Torin 1 mw the Tat pathway’s main raison d’être and demonstrates a critical role for the Tat pathway in the biosynthesis of noncytoplasmic metalloproteins. Amongst the putative Tat substrates in cyanobacteria, several are predicted or known to bind metals and examples include FeS cluster containing proteins, such as PetC, molybdopterin-containing oxidoreductases, Mn-dependent superoxide dismutase and the zinc-dependent carbonic anhydrase. Each of these proteins must acquire its metal cofactor within the cytoplasm

before translocation can occur. The recent publication of complete genome sequences of a number of cyanobacterial species has opened the door to new and detailed genomic and proteomic investigations of protein targeting in cyanobacteria. Given their significance in terms of global photosynthetic activity and primary production, a fundamental understanding of cell function in general will be of great benefit. The use of advanced

bio-imaging techniques and proteomics should help us to unravel the secrets of protein sorting in cyanobacteria whose unique cellular organization amongst prokaryotes provides an intriguing layer of complexity. The significance of the Tat pathway in metalloprotein assembly selleck chemical and export is also beginning to be unravelled and recent advances in bioinorganic chemistry, including metalloproteomics, are opening new avenues of enquiry. The authors acknowledge the support of the Leverhulme Trust. “
“Bc1245 is a monocistronic chromosomal gene of Bacillus cereus ATCC 14579 encoding a putative protein of 143 amino acids identified in this study to have a spore-related function in B. cereus. Bc1245 is highly conserved in the genome of members of the B. cereus group, indicating

an important function of the gene in this group of bacteria. Quantitative PCR revealed that bc1245 is transcribed late in sporulation (upon formation of phase-bright spores) and at the same time as the mother cell–specific transcription factor σK. The σK regulon Adenosine triphosphate includes structural components of the spore (such as coat proteins), and it is therefore plausible that bc1245 might encode a structural outer spore protein. This was confirmed by detection of BC1245 in exosporium extracts from B. cereus by immunoblotting against BC1245 antiserum. Bacillus encompasses species capable of forming highly resistant dormant endospores as a response to environmental stress such as nutrient deprivation (Setlow & Johnson, 2007, and references therein). When receiving a specific signal (nutrient or nonnutrient derived), spores are able to come back to life as vegetative cells in an irreversible process called germination and subsequent outgrowth (Moir et al., 2002; Setlow, 2003).

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