scholarly journals A Radical Clock Probe Uncouples H Atom Abstraction from Thioether Cross-Link Formation by the Radical S-Adenosyl-l-methionine Enzyme SkfB

Biochemistry ◽  
2018 ◽  
Vol 57 (32) ◽  
pp. 4816-4823 ◽  
Author(s):  
William M. Kincannon ◽  
Nathan A. Bruender ◽  
Vahe Bandarian
Keyword(s):  
Cross Link ◽  
Radical Clock ◽  
Link Formation

Mechanisms of DNA−protein cross-link formation and repair

2021 ◽  
pp. 140669
Author(s):  
Xiaoying Wei ◽  
Ying Peng ◽  
Cameron Bryan ◽  
Kun Yang
Keyword(s):  
Cross Link ◽  
Link Formation

scholarly journals Hypoxia-Selective DNA Interstrand Cross-Link Formation by Two Modified Nucleosides

2012 ◽  
Vol 18 (40) ◽  
pp. 12609-12613 ◽  
Author(s):  
Yunyan Kuang ◽  
Huabing Sun ◽  
J. Craig Blain ◽  
Xiaohua Peng
Keyword(s):  
Modified Nucleosides ◽  
Cross Link ◽  
Link Formation

scholarly journals Osteoarthritis-related fibrosis is associated with both elevated pyridinoline cross-link formation and lysyl hydroxylase 2b expression

2013 ◽  
Vol 21 (1) ◽  
pp. 157-164 ◽  
Author(s):  
D.F.G. Remst ◽  
E.N. Blaney Davidson ◽  
E.L. Vitters ◽  
A.B. Blom ◽  
R. Stoop ◽  
...  
Keyword(s):  
Cross Link ◽  
Lysyl Hydroxylase ◽  
Link Formation

scholarly journals Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation

2018 ◽  
Vol 54 (49) ◽  
pp. 6296-6299 ◽  
Author(s):  
Suresh S. Pujari ◽  
Yi Zhang ◽  
Shaofei Ji ◽  
Mark D. Distefano ◽  
Natalia Y. Tretyakova
Keyword(s):  
Cross Linking ◽  
Cross Link ◽  
Site Specific ◽  
Link Formation

Model site-specific DNA–protein cross-link formation by bioorthogonal oxime ligation.

scholarly journals Two DD-Carboxypeptidases fromMycobacterium smegmatisAffect Cell Surface Properties through Regulation of Peptidoglycan Cross-Linking and Glycopeptidolipids

2018 ◽  
Vol 200 (14) ◽  
Author(s):  
Satya Deo Pandey ◽  
Shilpa Pal ◽  
Ganesh Kumar N ◽  
Ankita Bansal ◽  
Sathi Mallick ◽  
...  
Keyword(s):  
Cell Surface ◽  
Mycobacterium Smegmatis ◽  
Biofilm Formation ◽  
Cross Linking ◽  
Surface Lipid ◽  
Cross Link ◽  
Content Type ◽  
Murine Macrophages ◽  
Cross Links ◽  
Link Formation

ABSTRACTDuring the peptidoglycan (PG) maturation of mycobacteria, the glycan strands are interlinked by both 3-3 (between twomeso-diaminopimelic acids [meso-DAPs]) and 4-3 cross-links (betweend-Ala andmeso-DAP), though there is a predominance (60 to 80%) of 3-3 cross-links. Thedd-carboxypeptidases (dd-CPases) act on pentapeptides to generate tetrapeptides that are used byld-transpeptidases as substrates to form 3-3 cross-links. Therefore,dd-CPases play a crucial role in mycobacterial PG cross-link formation. However, the physiology ofdd-CPases in mycobacteria is relatively unexplored. In this study, we deleted twodd-CPase genes,msmeg_2433andmsmeg_2432, both individually and in combination, fromMycobacterium smegmatismc2155. Though the singledd-CPase gene deletions had no significant impact on the mycobacterial physiology, many interesting functional alterations were observed in the double-deletion mutant,viz., a predominance in PG cross-link formation was shifted from 3-3 cross-links to 4-3, cell surface glycopeptidolipid (GPL) expression was reduced, and susceptibility to β-lactams and antitubercular agents was enhanced. Moreover, the survival rate of the double mutant within murine macrophages was higher than that of the parent. Interestingly, the complementation with any one of thedd-CPase genes could restore the wild-type phenotype. In a nutshell, we infer that the altered ratio of 4-3 to 3-3 PG cross-links might have influenced the expression of surface GPLs, colony morphology, biofilm formation, drug susceptibility, and subsistence of the cells within macrophages.IMPORTANCEThe glycan strands in mycobacterial peptidoglycan (PG) are interlinked by both 3-3 and 4-3 cross-links. Thedd-CPases generate tetrapeptides by acting on the pentapeptides, andld-transpeptidases use tetrapeptides as substrates to form 3-3 cross-links. In this study, we showed that simultaneous deletions of twodd-CPases alter the nature of PG cross-linking from 3-3 cross-links to 4-3 cross-links. The deletions subsequently decrease the expression of glycopeptidolipids (significant surface lipid present in many nontuberculous mycobacteria, includingMycobacterium smegmatis) and affect other physiological parameters, like cell morphology, growth rate, biofilm formation, antibiotic susceptibility, and survival within murine macrophages. Thus, unraveling the physiology ofdd-CPases might help us design antimycobacterial therapeutics in the future.

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