Two genes present on a transposon-like structure in Lactococcus lactis are involved in a Clp-family proteolytic activity |
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| Authors: | Dao Chao Huang Xian Fang Huang Georges Novel Madeleine Novel |
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| Institution: | Laboratoire de Génétique Microbienne, institut de Recherche en Biologie Appliquée (IRBA), Universitéde Caen, 14032 Caen Cedex, France. |
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| Abstract: | The lactose-protease plasmid pUCL22 of Lactococcus lactis subsp. lactis strain CNRZ270 contained two inverted copies of IS 1076 flanking a region of 3.7 kb. This internal region was sequenced and found to contain two large open reading frames, ORF1 and ORFP in opposite orientations. ORF1 consists of 2289 bp; the deduced 763-amino-acid sequence is similar to the ATPases of the ClpA family. It contains two well-conserved consensus ATP-binding sites. It was named ClpL. ORFP consists of 930 bp encoding a protein of 310 amino acids. No similarity with any known protein was found in GenBank data for ORFP. Increased ATP-dependent proteolytic activity was detected in extracts from Escherichia coli cells expressing the clpL and ORFP genes. |
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