Cloning and sequence analysis of a signal peptidase I from the thermophilic cyanobacterium Phormidium laminosum |
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Authors: | Jeremy C. L. Packer Dominique André Christopher J. Howe |
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Affiliation: | (1) Department of Biochemistry, University of Cambridge, Tennis Court Road, CB2 1QW Cambridge, UK;(2) Cambridge Centre for Molecular Recognition, University of Cambridge, Tennis Court Road, CB2 1QW Cambridge, UK |
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Abstract: | Type I signal peptidases are a widespread family of enzymes which remove the presequences from proteins translocated across cell membranes, including thylakoid and cytoplasmic membranes of cyanobacteria and thylakoid membranes of chloroplasts. We have cloned and sequenced a signal peptidase gene from the thermophilic cyanobacterium Phormidium laminosum which is believed to encode an enzyme common to both membrane systems. The deduced amino acid sequence is 203 residues long and although the overall similarity among signal peptidases is rather low there are a number of identifiable conserved regions present. The P. laminosum enzyme is predicted to have a single transmembrane domain, in contrast to other Gram-negative bacterial sequences, but similar to other type I signal peptidases. |
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Keywords: | Phormidium laminosum cyanobacteria signal peptidase protein targeting |
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