Enzymatic characterization of a lysin encoded by bacteriophage EL.
The bacteriophage EL is a virus that specifically attacks the human pathogenPseudomonas aeruginosa. This phage carries a large genome that encodes for its own chaperonin which presumably facilitates the proper folding of phage proteins independently of the host chaperonin system. EL also encodes a lysin enzyme, a critical component of the lytic cycle that is responsible for digesting the peptidoglycan layer of the host cell wall. Previously, this lysin was believed to be a substrate of the chaperonin encoded by phage EL. In order to characterize the activity of the EL lysin, and to determine whether lysin activity is contingent on chaperonin-mediated folding, a series of peptidoglycan hydrolysis activity assays were performed. Results indicate that the EL-encoded lysin has similar enzymatic activity to that of theGallus gallus lysozymeand that the EL lysin folds into a functional enzyme in the absence of phage chaperonin and should not be considered a substrate.
Department of Chemistry; University of Texas at El Paso; El Paso, TX USA.
Diana A
DA
Tafoya
Zacariah L
ZL
Hildenbrand
Nadia
N
Herrera
Sudheer K
SK
Molugu
Vadim V
VV
Mesyanzhinov
Konstantin A
KA
Miroshnikov
Ricardo A
RA
Bernal
bacteriophage EL; chaperonin; lysin; lysozyme; protein folding