In silico identification and characterization of sensory motifs in the transcriptional regulators of the ArsR-SmtB family

Metallomics ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1476-1500 ◽  
Author(s):  
Rima Roy ◽  
Saikat Samanta ◽  
Surajit Patra ◽  
Nav Kumar Mahato ◽  
Rudra P. Saha

The ArsR-SmtB family of transcriptional repressors regulates the transcription of metal-efflux proteins by binding specific metals at a variety of secondary structural elements, called motifs, on the surface of the proteins.

2019 ◽  
Vol 42 (1) ◽  
pp. 68-73
Author(s):  
Cássia Alves Lima-Rezende ◽  
Gislaine Aparecida Fernandes ◽  
Helder Elias da Silva ◽  
Sarah Dobkowski-Marinho ◽  
Victor Fernandes Santos ◽  
...  

2001 ◽  
Vol 183 (16) ◽  
pp. 4779-4785 ◽  
Author(s):  
Q. May Wang ◽  
Robert B. Peery ◽  
Robert B. Johnson ◽  
William E. Alborn ◽  
Wu-Kuang Yeh ◽  
...  

ABSTRACT A gene (mgt) encoding a monofunctional glycosyltransferase (MGT) from Staphylococcus aureus has been identified. This first reported gram-positive MGT shared significant homology with several MGTs from gram-negative bacteria and the N-terminal glycosyltransferase domain of class A high-molecular-mass penicillin-binding proteins from different species.S. aureus MGT contained an N-terminal hydrophobic domain perhaps involved with membrane association. It was expressed inEscherichia coli cells as a truncated protein lacking the hydrophobic domain and purified to homogeneity. Analysis by circular dichroism revealed that secondary structural elements of purified truncated S. aureus MGT were consistent with predicted structural elements, indicating that the protein might exhibit the expected folding. In addition, purified S. aureus MGT catalyzed incorporation of UDP-N-acetylglucosamine into peptidoglycan, proving that it was enzymatically active. MGT activity was inhibited by moenomycin A, and the reaction product was sensitive to lysozyme treatment. Moreover, a protein matching the calculated molecular weight ofS. aureus MGT was identified from an S. aureus cell lysate using antibodies developed against purified MGT. Taken together, our results suggest that this enzyme is natively present in S. aureus cells and that it may play a role in bacterial cell wall biosynthesis.


2016 ◽  
Vol 92 ◽  
pp. 11-18 ◽  
Author(s):  
Álvaro Labra ◽  
Oscar Arredondo-Zelada ◽  
Patricio Flores-Herrera ◽  
Sergio H. Marshall ◽  
Fernando A. Gómez

Plant Gene ◽  
2021 ◽  
pp. 100280
Author(s):  
Tushar Khare ◽  
Shrushti Joshi ◽  
Kawaljeet Kaur ◽  
Amrita Srivastav ◽  
Varsha Shriram ◽  
...  

IUBMB Life ◽  
2020 ◽  
Vol 72 (5) ◽  
pp. 991-1000
Author(s):  
Elaheh Zadeh Hosseingholi ◽  
Neda Neghabi ◽  
Ghader Molavi ◽  
Seyed Mohammad Gheibi Hayat ◽  
Hamed Shahriarpour

Genomics ◽  
2018 ◽  
Vol 110 (1) ◽  
pp. 23-34
Author(s):  
Gourab Das ◽  
Surojit Das ◽  
Shanta Dutta ◽  
Indira Ghosh

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