Characterization of anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate plugin

Binh V. Le; Jennifer B. Nguyen; Shankar Logarajah; Bo Wang; Jacob Marcus; Hazel P. Williams; Flaminia Catteruccia; Richard H.G. Baxter

doi:10.1074/jbc.M112.435347

Characterization of anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate plugin

Binh V. Le, Jennifer B. Nguyen, Shankar Logarajah, Bo Wang, Jacob Marcus, Hazel P. Williams, Flaminia Catteruccia, Richard H.G. Baxter

Cancer Signaling and Microenvironment (CSM)

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Background: A. gambiae transglutaminase AgTG3 cross-links Plugin within seminal fluids. Results: AgTG3 and Plugin were purified and their structure and activity characterized in vitro. Conclusion: AgTG3 forms a dimer in solution, analogous to human FXIII. Plugin is nonglobular in solution. AgTG3 is Ca dependent and prefers Plugin as a substrate. Significance: Inhibition of AgTG3 cross-linking of Plugin is a possible method to chemosterilize male Anopheles mosquitoes.

Original language	English
Pages (from-to)	4844-4853
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	7
DOIs	https://doi.org/10.1074/jbc.M112.435347
State	Published - Feb 15 2013

Keywords

Amino Acid Sequence
Animals
Anopheles/enzymology
Calcium/chemistry
Cross-Linking Reagents/chemistry
Cytoplasm/metabolism
Dimerization
Female
Male
Mass Spectrometry/methods
Models, Chemical
Molecular Sequence Data
Peptides/chemistry
Protein Binding
Protein Glutamine gamma Glutamyltransferase 2
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Structure-Activity Relationship
Transglutaminases/chemistry

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10.1074/jbc.M112.435347

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title = "Characterization of anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate plugin",

abstract = "Background: A. gambiae transglutaminase AgTG3 cross-links Plugin within seminal fluids. Results: AgTG3 and Plugin were purified and their structure and activity characterized in vitro. Conclusion: AgTG3 forms a dimer in solution, analogous to human FXIII. Plugin is nonglobular in solution. AgTG3 is Ca dependent and prefers Plugin as a substrate. Significance: Inhibition of AgTG3 cross-linking of Plugin is a possible method to chemosterilize male Anopheles mosquitoes.",

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author = "Le, {Binh V.} and Nguyen, {Jennifer B.} and Shankar Logarajah and Bo Wang and Jacob Marcus and Williams, {Hazel P.} and Flaminia Catteruccia and Baxter, {Richard H.G.}",

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doi = "10.1074/jbc.M112.435347",

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journal = "Journal of Biological Chemistry",

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AU - Le, Binh V.

AU - Nguyen, Jennifer B.

AU - Logarajah, Shankar

AU - Wang, Bo

AU - Marcus, Jacob

AU - Williams, Hazel P.

AU - Catteruccia, Flaminia

AU - Baxter, Richard H.G.

PY - 2013/2/15

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N2 - Background: A. gambiae transglutaminase AgTG3 cross-links Plugin within seminal fluids. Results: AgTG3 and Plugin were purified and their structure and activity characterized in vitro. Conclusion: AgTG3 forms a dimer in solution, analogous to human FXIII. Plugin is nonglobular in solution. AgTG3 is Ca dependent and prefers Plugin as a substrate. Significance: Inhibition of AgTG3 cross-linking of Plugin is a possible method to chemosterilize male Anopheles mosquitoes.

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KW - Amino Acid Sequence

KW - Animals

KW - Anopheles/enzymology

KW - Calcium/chemistry

KW - Cross-Linking Reagents/chemistry

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KW - Male

KW - Mass Spectrometry/methods

KW - Models, Chemical

KW - Molecular Sequence Data

KW - Peptides/chemistry

KW - Protein Binding

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KW - Protein Structure, Tertiary

KW - Sequence Homology, Amino Acid

KW - Structure-Activity Relationship

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IS - 7

ER -

Characterization of anopheles gambiae transglutaminase 3 (AgTG3) and its native substrate plugin

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Keywords

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