TY  - JOUR
A1  - Grabarczyk, Daniel B.
A1  - Berks, Ben C.
T1  - Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ
JF  - PLoS ONE
N2  - The Sox pathway found in many sulfur bacteria oxidizes thiosulfate to sulfate. Pathway intermediates are covalently bound to a cysteine residue in the carrier protein SoxYZ. We have used biochemical complementation by SoxYZ-conjugates to probe the identity of the intermediates in the Sox pathway. We find that unconjugated SoxYZ and SoxYZ-S-sulfonate are unlikely to be intermediates during normal turnover in disagreement with current models. By contrast, conjugates with multiple sulfane atoms are readily metabolised by the Sox pathway. The most parsimonious interpretation of these data is that the true carrier species in the Sox pathway is a SoxYZ-S-sulfane adduct.
KW  - thiosulfates
KW  - oxidation
KW  - sulfur
KW  - cysteine
KW  - sulfides
KW  - thermodynamics
KW  - sulfates
KW  - sulfites
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-171147
VL  - 12
IS  - 3
ER  - 
TY  - JOUR
A1  - Peissert, Stefan
A1  - Sauer, Florian
A1  - Grabarczyk, Daniel B.
A1  - Braun, Cathy
A1  - Sander, Gudrun
A1  - Poterszman, Arnaud
A1  - Egly, Jean-Marc
A1  - Kuper, Jochen
A1  - Kisker, Caroline
T1  - In TFIIH the Arch domain of XPD is mechanistically essential for transcription and DNA repair
JF  - Nature Communications
N2  - The XPD helicase is a central component of the general transcription factor TFIIH which plays major roles in transcription and nucleotide excision repair (NER). Here we present the high-resolution crystal structure of the Arch domain of XPD with its interaction partner MAT1, a central component of the CDK activating kinase complex. The analysis of the interface led to the identification of amino acid residues that are crucial for the MAT1-XPD interaction. More importantly, mutagenesis of the Arch domain revealed that these residues are essential for the regulation of (i) NER activity by either impairing XPD helicase activity or the interaction of XPD with XPG; (ii) the phosphorylation of the RNA polymerase II and RNA synthesis. Our results reveal how MAT1 shields these functionally important residues thereby providing insights into how XPD is regulated by MAT1 and defining the Arch domain as a major mechanistic player within the XPD scaffold.
KW  - nucleotide excision repair
KW  - nuclear receptors
KW  - helicase
KW  - transactivation
KW  - fluorescence
KW  - recognition
KW  - subunit
KW  - binding
KW  - sulfur
KW  - kinease
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-229857
VL  - 11
IS  - 1
ER  -