A natural SNP variant in sulfite reductase influences sulfur assimilation in maize

2021 ◽  
Author(s):  
Luguang Jiang ◽  
Yan Wang ◽  
Aiai Xia ◽  
Qi Wang ◽  
Xiaolei Zhang ◽  
...  
2012 ◽  
Vol 83 ◽  
pp. 34-42 ◽  
Author(s):  
Michael T. McManus ◽  
Srishti Joshi ◽  
Bruce Searle ◽  
Meeghan Pither-Joyce ◽  
Martin Shaw ◽  
...  

2021 ◽  
Vol 213 (2) ◽  
pp. 107724
Author(s):  
Daniel T. Murray ◽  
Kevin L. Weiss ◽  
Christopher B. Stanley ◽  
Gergely Nagy ◽  
M. Elizabeth Stroupe

2021 ◽  
Author(s):  
Lei Hua ◽  
Sean R. Stevenson ◽  
Ivan Reyna‐Llorens ◽  
Haiyan Xiong ◽  
Stanislav Kopriva ◽  
...  

1999 ◽  
Vol 63 (4) ◽  
pp. 762-766 ◽  
Author(s):  
Yube YAMAGUCHI ◽  
Tatsuo NAKAMURA ◽  
Emiko HARADA ◽  
Nozomu KOIZUMI ◽  
Hiroshi SANO

Microbiology ◽  
2004 ◽  
Vol 150 (6) ◽  
pp. 1681-1686 ◽  
Author(s):  
Rachel Pinto ◽  
Quing Xui Tang ◽  
Warwick J. Britton ◽  
Thomas S. Leyh ◽  
James A. Triccas

Sulfur metabolism has been implicated in the virulence, antibiotic resistance and anti-oxidant defence of Mycobacterium tuberculosis. Despite its human disease relevance, sulfur metabolism in mycobacteria has not yet been fully characterized. ATP sulfurylase catalyses the synthesis of activated sulfate (adenosine 5′-phosphosulfate, APS), the first step in the reductive assimilation of sulfate. Expression of the M. tuberculosis cysD gene, predicted to encode the adenylyl-transferase subunit of ATP sulfurylase, is upregulated by the bacilli inside its preferred host, the macrophage. This study demonstrates that cysD and cysNC orthologues exist in M. tuberculosis and constitute an operon whose expression is induced by sulfur limitation and repressed by the presence of cysteine, a major end-product of sulfur assimilation. The cysDNC genes are also induced upon exposure to oxidative stress, suggesting regulation of sulfur assimilation by M. tuberculosis in response to toxic oxidants. To ensure that the cysDNC operon encoded the activities predicted by its primary sequence, and to begin to characterize the products of the operon, they were expressed in Escherichia coli, purified to homogeneity, and tested for their catalytic activities. The CysD and CysNC proteins were shown to form a multifunctional enzyme complex that exhibits the three linked catalytic activities that constitute the sulfate activation pathway.


Biochemistry ◽  
1989 ◽  
Vol 28 (13) ◽  
pp. 5477-5485 ◽  
Author(s):  
Sanghwa Han ◽  
John F. Madden ◽  
Lewis M. Siegel ◽  
Thomas G. Spiro

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