1887

Abstract

The BofA protein is involved in regulation of pro-σ processing in the mother cell during the late stages of sporulation. A computer analysis of the BofA amino acid sequence indicates that it is an integral membrane protein. To determine the membrane topology of the protein, a series of gene fusions of with or reporter genes in were analysed. A BofA topological model with two membrane-spanning segments, and with the N- and the C-terminal domains located in the region between the inner and outer membranes surrounding the forespore is presented. The analysis of different modifications of the last five amino acid residues of the BofA protein, obtained by PCR site-directed mutagenesis, suggests a possible role of the C-terminal domain in the regulation of pro-σ processing.

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/content/journal/micro/10.1099/00221287-143-4-1053
1997-04-01
2019-10-13
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-143-4-1053
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