Open AccessThe actin‐polymerization protein from Listeria ivanovii is a large repeat protein which shows only limited amino acid sequence homology to actA from Listeria monocytogenes
Author(s) -
Kreft Jürgen,
Dumbsky Martina,
Theiss Stephanie
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07403.x
Subject(s) - listeria monocytogenes , gene , homology (biology) , biology , peptide sequence , gene product , actin , nucleic acid sequence , amino acid , listeria , genetics , biochemistry , bacteria , gene expression
Within infected eukaryotic cells the two pathogenic Listeria species, L. monocytogenes and L. ivanovii , induce polymerization of cellular actin and the formation of a propulsive actin tail at one bacterial pole. For L. monocytogenes it has been shown that the product of the listerial actA gene is required for this process which is regarded as a model for actin‐based motility. We have now cloned and sequenced a functionally analogous gene from L. ivanovii ; its product, as deduced from the DNA sequence, is considerably larger (108 kDa) than L. monocytogenes ActA (67 kDa) and shares only a limited amino acid sequence homology (46% similarity on average) with the latter protein. This is the first example of a virulence gene product from L. ivanovii which is significantly different from its L. monocytogenes counterpart. Comparison of the two ActA proteins gives new insight into the structure of this class of actin‐polymerization proteins, in particular with respect to their proline‐rich repeat region.