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      Identification of the proteome complement of hypopharyngeal glands from two strains of honeybees (Apis mellifera)

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      Apidologie
      EDP Sciences

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          Structure, mechanism and regulation of peroxiredoxins

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            A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation.

            The Yap1 transcription factor regulates hydroperoxide homeostasis in S. cerevisiae. Yap1 is activated by oxidation when hydroperoxide levels increase. We show that Yap1 is not directly oxidized by hydroperoxide. We identified the glutathione peroxidase (GPx)-like enzyme Gpx3 as a second component of the pathway, serving the role of sensor and transducer of the hydroperoxide signal to Yap1. When oxidized by H2O2, Gpx3 Cys36 bridges Yap1 Cys598 by a disulfide bond. This intermolecular disulfide bond is then resolved into a Yap1 intramolecular disulfide bond, the activated form of the regulator. Thioredoxin turns off the pathway by reducing both sensor and regulator. These data reveal a redox-signaling function for a GPx-like enzyme and elucidate a eukaryotic hydroperoxide-sensing mechanism. Gpx3 is thus a hydroperoxide receptor and redox-transducer.
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              Regulation of honey bee division of labor by colony age demography

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                Author and article information

                Journal
                Apidologie
                Apidologie
                EDP Sciences
                0044-8435
                1297-9678
                March 2008
                February 9 2008
                March 2008
                : 39
                : 2
                : 199-214
                Article
                10.1051/apido:2007059
                88aa8a5c-51cf-4b4e-89d3-1b2fa97d59a8
                © 2008
                History

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