Differences in the regulation of cytochrome P450 family members during liver regeneration

1997 ◽  
Vol 26 (1) ◽  
pp. 48-54 ◽  
Author(s):  
Christian Trautwein ◽  
Tim Rakemann ◽  
Petra Obermayer-Straub ◽  
Monika Niehof ◽  
Michael Peter Manns
2013 ◽  
Vol 28 (2) ◽  
pp. 966-977 ◽  
Author(s):  
Carlos G. Penaloza ◽  
Brian Estevez ◽  
Dinah M. Han ◽  
Melissa Norouzi ◽  
Richard A. Lockshin ◽  
...  

Author(s):  
Xiupeng Mei ◽  
Jin Nan ◽  
Zikun Zhao ◽  
Shun Yao ◽  
Wenqin Wang ◽  
...  

Abstract Leaf angle (LA) and leaf orientation value (LOV) are critical agronomic traits for maize plant architecture. Many genes related to plant architecture have been identified in maize, but the functions of NF-Y members in regulating plant architecture have not been reported before. Here, we identified a regulator of maize plant architecture, ZmNF-YC13. ZmNF-YC13 was highly expressed in the leaf base zone of maize plants. ZmNF-YC13 overexpression plants showed upright leaves with narrow LA and larger LOV, while ZmNF-YC13 knockout plants had larger LA and smaller LOV, compared with wild-type plants. The changes in plant architecture were due to the changes of the expression levels of cytochrome P450 family members. ZmNF-YC13 can interact with two ZmNF-YBs (ZmNF-YB9 and ZmNF-YB10) of the LEC1 subfamily, and further recruit ZmNF-YA3 to form two NF-Y complexes. The two complexes can both activate the promoters of the transcriptional repressors (ZmWRKY76 and ZmBT2) and the promoters of PLA cluster gene can be repressed by ZmWRKY76 and ZmBT2 in maize protoplasts. We propose that ZmNF-YC13 functions as a transcriptional regulator and, together with ZmNF-YBs and ZmNF-YA3, affects plant architecture by regulating the expression of ZmWRKY76 and ZmBT2, which repress the expression of PLA clustered cytochrome P450 family members.


2018 ◽  
Vol 475 (23) ◽  
pp. 3875-3886 ◽  
Author(s):  
Craig S. Robb ◽  
Lukas Reisky ◽  
Uwe T. Bornscheuer ◽  
Jan-Hendrik Hehemann

Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily.


2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Guillaume Bordet ◽  
Niraj Lodhi ◽  
Danping Guo ◽  
Andrew Kossenkov ◽  
Alexei V. Tulin

AbstractPoly(ADP-ribose) polymerase 1 (PARP-1) is a nuclear enzyme involved in DNA repair and transcription regulation, among other processes. Malignant transformations, tumor progression, the onset of some neuropathies and other disorders have been linked to misregulation of PARP-1 activity. Despite intensive studies during the last few decades, the role of PARP-1 in transcription regulation is still not well understood. In this study, a transcriptomic analysis in Drosophila melanogaster third instar larvae was carried out. A total of 602 genes were identified, showing large-scale changes in their expression levels in the absence of PARP-1 in vivo. Among these genes, several functional gene groups were present, including transcription factors and cytochrome family members. The transcription levels of genes from the same functional group were affected by the absence of PARP-1 in a similar manner. In the absence of PARP-1, all misregulated genes coding for transcription factors were downregulated, whereas all genes coding for members of the cytochrome P450 family were upregulated. The cytochrome P450 proteins contain heme as a cofactor and are involved in oxidoreduction. Significant changes were also observed in the expression of several mobile elements in the absence of PARP-1, suggesting that PARP-1 may be involved in regulating the expression of mobile elements.


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