ArticlePloS one2011
The C-terminal domain of the novel essential protein Gcp is critical for interaction with another essential protein YeaZ of Staphylococcus aureus.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- The Impacts of Essential Gcp/TsaD Protein on Cell Morphology, Virulence Expression, and Antibiotic Susceptibility inMicroorganisms · 2025Article
- New Insights into the Biological Functions of Essential TsaB/YeaZ Protein inAntibiotics (Basel, Switzerland) · 2024Article
- Article
- Determination of essentiality and regulatory function of staphylococcal YeaZ in branched-chain amino acid biosynthesis.Virulence · 2015Article
- Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex.Protein science : a publication of the Protein Society · 2013Article
- Antisense RNA regulation and application in the development of novel antibiotics to combat multidrug resistant bacteria.Science progress · 2013Review
- Deinococcus radiodurans YgjD and YeaZ are involved in the repair of DNA cross-links.Extremophiles : life under extreme conditions · 2013Article
- Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside.The Journal of biological chemistry · 2012Article
- The essentiality of staphylococcal Gcp is independent of its repression of branched-chain amino acids biosynthesis.PloS one · 2012Article
- Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies have demonstrated that the novel protein Gcp is essential for the viability of various bacterial species including Staphylococcus aureus; however, the reason why it is required for bacterial growth remains unclear. In order to explore the potential mechanisms of this essentiality, we performed RT-PCR analysis and revealed that the gcp gene (sa1854) was co-transcribed with sa1855, yeaZ (sa1856) and sa1857 genes, indicating these genes are located in the same operon. Furthermore, we demonstrated that Gcp interacts with YeaZ using a yeast two-hybrid (Y2H) system and in vitro pull down assays. To characterize the Gcp-YeaZ interaction, we performed alanine scanning mutagenesis on the residues of C-terminal segment of Gcp. We found that the mutations of the C-terminal Y317-F322 region abolished the interaction of Gcp and YeaZ, and the mutations of the D324-N329 and S332-Y336 regions alleviated Gcp binding to YeaZ. More importantly, we demonstrated that these key regions of Gcp are also necessary for the bacterial survival since these mutated Gcp could not complement the depletion of endogenous Gcp. Taken together, our data suggest that the interaction of Gcp and YeaZ may contribute to the essentiality of Gcp for S. aureus survival. Our findings provide new insights into the potential mechanisms and biological functions of this novel essential protein.
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