Murein-hydrolyzing activity of flagellin FlaA of Listeria monocytogenes.
In this preliminary report we show that a 29 kDa surface protein of Listeria monocytogenes EGD removed from cells with 4 M LiCl has peptidoglycan (murein) hydrolyzing activity, as revealed by zymographic analysis using Bacillus subtilis murein and heat-killed Micrococcus luteus cells casted in the gel. Following two-dimensional electrophoresis, the protein was electroblotted to PVDF membrane and its identity (FlaA) was revealed by sequencing. Peptidoglycan hydrolysing activity of FlaA purified by FPLC on Mono-S Sepharose against labelled Escherichia coli murein was demonstrated.
Popowska
Magdalena
M
Department of Bacterial Physiology, Institute of Microbiology, Warsaw University Miecznikowa 1, 02-096 Warsaw, Poland. magdapop@biol.uw.edu.pl
Markiewicz
Zdzislaw
Z
D002846:Chromatography, Affinity; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000378:metabolism; D005408:Flagellin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000201:enzymology*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism
D010457:Peptidoglycan; D005408:Flagellin; C067138:flaA protein, bacteria; D009238:N-Acetylmuramoyl-L-alanine Amidase