Characterization of Burkholderia pseudomallei protein BPSL1375 validates the Putative hemolytic activity of the COG3176 N-Acyltransferase family
Background: There are still numerous protein subfamilies within families and superfamilies that do not yet have conclusive empirical experimental evidence providing a specific function. These proteins persist in databases with the annotation of a specific ‘putative’ function made by association wi...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BioMed Central Ltd
2015
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| Subjects: | |
| Online Access: | http://eprints.intimal.edu.my/226/1/Characterization%20of%20Burkholderia.pdf http://eprints.intimal.edu.my/226/ http://www.biomedcentral.com/ |
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| Summary: | Background: There are still numerous protein subfamilies within families and superfamilies that do not yet have
conclusive empirical experimental evidence providing a specific function. These proteins persist in databases with
the annotation of a specific ‘putative’ function made by association with discernible features in the protein
sequence.
Results: Here, we report the characterization of one such protein produced by the pathogenic soil bacterium
Burkholderia pseudomallei, BPSL1375, which provided evidence for putative hemolysins in the COG3176 family to
have experimentally validated hemolytic activity. BPSL1375 can be classified into the N-acyltransferase superfamily,
specifically to members of the COG3176 family. Sequence alignments identified seven highly conserved residues
(Arg54, Phe58, Asp75, Asp78, Arg99, Glu132 and Arg135), of which several have been implicated with Nacyltransferase
activity in previously characterized examples. Using the 3D model of an N-acyltransferase example as
a reference, an acyl homoserine lactone synthase, we generated 3D structure models for mutants of six of the
seven N-acyltransferase conserved residues (R54, D75, D78, R99, E132 and R135). Both the R99 and R135 mutants
resulted in a loss of hemolytic activity while mutations at the other five positions resulted in either reduction or
increment in hemolytic activity.
Conclusions: The implication of residues previously characterized to be important for N-acyltransferase activity to
hemolytic activity for the COG3176 family members of the N-acyltransferase provides validation of the correct
placement of the hemolytic capability annotation within the N-acyltransferase superfamily. |
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