Der Blaulicht-Photorezeptor Cryptochrom 2 aus Arabidopsis thaliana: Lichtabhängige Phosphorylierung und Interaktionspartner in der Signaltransduktion
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Philipps-Universität Marburg
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Abstract
Althougth the physiological functions of plant
cryptochromes have been thoroughly investigated and their near
relatives, the photolyases have been studied on the molecular
level in very detail, the knowledge about the signal
transduction of the cryptochromes however is relatively poor.
Following the aim to find out more about these molecular
processes, this work presents insights into some aspects, using
Arabidopsis cry2 as a model. In this thesis, a light dependent
posphorylation of cry2 has been discovered and further
investigated. The recorded action-spectrum of this
phosphorylation shows clear characteristics of a
flavin-spectrum. Attempts to identifiy the responsible kinase
have not been finished so far. A potential autophosphorylation
activity connected with cry2 has been discussed, but could not
be proven, finally. Further experiments with heterologouesly
expressed cry2 in yeast resulted in data that suggest a role of
cry2 as light dependent transcription activator. Also a
DNA-binding activity of in vitro-transcribed and -translated
cry2 has been demonstrated.
Furthermore, the subcellular
localization of two putative interaction partners of cry2
? At5g26280 and At2g02230 - has been described. At2g02230
has been identified as functional F-box protein. Studies to
elucidate the degradation pathway of cry2 could not strengthen
the model of a proteasomal degradation.Althougth the physiological functions of plant
cryptochromes have been thoroughly investigated and their near
relatives, the photolyases have been studied on the molecular
level in very detail, the knowledge about the signal
transduction of the cryptochromes however is relatively poor.
Following the aim to find out more about these molecular
processes, this work presents insights into some aspects, using
Arabidopsis cry2 as a model. In this thesis, a light dependent
posphorylation of cry2 has been discovered and further
investigated. The recorded action-spectrum of this
phosphorylation shows clear characteristics of a
flavin-spectrum. Attempts to identifiy the responsible kinase
have not been finished so far. A potential autophosphorylation
activity connected with cry2 has been discussed, but could not
be proven, finally. Further experiments with heterologouesly
expressed cry2 in yeast resulted in data that suggest a role of
cry2 as light dependent transcription activator. Also a
DNA-binding activity of in vitro-transcribed and -translated
cry2 has been demonstrated.
Furthermore, the subcellular
localization of two putative interaction partners of cry2
? At5g26280 and At2g02230 - has been described. At2g02230
has been identified as functional F-box protein. Studies to
elucidate the degradation pathway of cry2 could not strengthen
the model of a proteasomal degradation.
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Dates
Created: 2003Issued: 2003-12-22Updated: 2021-07-15
Faculty
Fachbereich Biologie
Publisher
Philipps-Universität Marburg
Language
ger
Data types
DoctoralThesis
Keywords
arabidopsissignal-transductioncryptochromephosphorylationflavin
DFG-subjects
FlavineSchmalwand CryptochromPhotorezeptorLichtabsorption
DDC-Numbers
570
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Müller, Markus Bernd (128590424): Der Blaulicht-Photorezeptor Cryptochrom 2 aus Arabidopsis thaliana: Lichtabhängige Phosphorylierung und Interaktionspartner in der Signaltransduktion. : Philipps-Universität Marburg 2003-12-22. DOI: https://doi.org/10.17192/z2003.0650.
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This item has been published with the following license: In Copyright