scholarly journals One evolutionarily selected amino acid variation is sufficient to provide functional specificity in the cold shock protein paralogs of Staphylococcus aureus

2020 ◽  
Vol 113 (4) ◽  
pp. 826-840 ◽  
Author(s):  
Arancha Catalan‐Moreno ◽  
Carlos J. Caballero ◽  
Naiara Irurzun ◽  
Sergio Cuesta ◽  
Jacinto López‐Sagaseta ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Cold Shock ◽  
Cold Shock Protein ◽  
Functional Specificity ◽  
Amino Acid Variation ◽  
Protein Paralogs

scholarly journals Characterization of an unusual cold shock protein from Staphylococcus aureus

2010 ◽  
Vol 50 (6) ◽  
pp. 519-526 ◽  
Author(s):  
Palas K. Chanda ◽  
Amitava Bandhu ◽  
Biswanath Jana ◽  
Rajkrishna Mondal ◽  
Tridib Ganguly ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cold Shock ◽  
Cold Shock Protein

scholarly journals CspA Regulates Pigment Production in Staphylococcus aureus through a SigB-Dependent Mechanism

2005 ◽  
Vol 187 (23) ◽  
pp. 8181-8184 ◽  
Author(s):  
Samuel Katzif ◽  
Eun-Hee Lee ◽  
Anthony B. Law ◽  
Yih-Ling Tzeng ◽  
William M. Shafer
Keyword(s):  
Staphylococcus Aureus ◽  
Sigma Factor ◽  
Cold Shock ◽  
Pigment Production ◽  
Cold Shock Protein ◽  
Alternative Sigma Factor ◽  
Expression Of Genes ◽  
Maximal Production ◽  
Dependent Mechanism

ABSTRACT We report that the cold shock protein CspA of Staphylococcus aureus is required for maximal production of pigment. Results from transcriptional studies revealed that loss of CspA resulted in decreased expression of genes needed for the biosynthesis of 4,4′-diaponeurosporene and the alternative sigma factor SigB.

scholarly journals Global effects of homocysteine on transcription in Escherichia coli: induction of the gene for the major cold-shock protein, CspA

Microbiology ◽  
2006 ◽  
Vol 152 (8) ◽  
pp. 2221-2231 ◽  
Author(s):  
Katy R. Fraser ◽  
Nina L. Tuite ◽  
Arvind Bhagwat ◽  
Conor P. O'Byrne
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Growth Medium ◽  
Amino Acid Metabolism ◽  
Cold Shock ◽  
Acid Metabolism ◽  
Cold Shock Protein ◽  
Rt Pcr ◽  
Life Threatening ◽  
The Impact

Homocysteine (Hcy) is a thiol-containing amino acid that is considered to be medically important because it is linked to the development of several life-threatening diseases in humans, including cardiovascular disease and stroke. It inhibits the growth of Escherichia coli when supplied in the growth medium. Growth inhibition is believed to arise as a result of partial starvation for isoleucine, which occurs because Hcy perturbs the biosynthesis of this amino acid. This study attempted to further elucidate the inhibitory mode of action of Hcy by examining the impact of exogenously supplied Hcy on the transcriptome. Using gene macroarrays the transcript levels corresponding to 68 genes were found to be reproducibly altered in the presence of 0.5 mM Hcy. Of these genes, the biggest functional groups affected were those involved in translation (25 genes) and in amino acid metabolism (19 genes). Genes involved in protection against oxidative stress were repressed in Hcy-treated cells and this correlated with a decrease in catalase activity. The gene showing the strongest induction by Hcy was cspA, which encodes the major cold-shock protein CspA. RT-PCR and reporter fusion experiments confirmed that cspA was induced by Hcy. Induction of cspA by Hcy was not caused by nutritional upshift, a stimulus known to induce CspA expression, nor was it dependent on the presence of a functional CspA protein. The induction of cspA by Hcy was suppressed when isoleucine was included in the growth medium. These data suggest that the induction of CspA expression in the presence of Hcy occurs because of a limitation for isoleucine. The possibility that Hcy-induced cspA expression is triggered by translational stalling that occurs when the cells are limited for isoleucine is discussed.

Study on the transgenic tobacco expressing truncated wheat cold shock protein gene TA3-13 and analysis of disease resistance

2011 ◽  
Vol 33 (5) ◽  
pp. 520-526 ◽  
Author(s):  
Na LI ◽  
Xiu-Zhen DU ◽  
Xiao-Mei PAN ◽  
Jin-Sheng WANG ◽  
Cong-Feng SONG
Keyword(s):  
Disease Resistance ◽  
Transgenic Tobacco ◽  
Cold Shock ◽  
Protein Gene ◽  
Cold Shock Protein

scholarly journals The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus

1967 ◽  
Vol 242 (20) ◽  
pp. 4736-4751
Author(s):  
Hiroshi Taniuchi ◽  
Christian B. Anfinsen ◽  
Ann Sodja
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Extracellular Nuclease

scholarly journals RNA thermoswitches modulate Staphylococcus aureus adaptation to ambient temperatures

2021 ◽  
Vol 49 (6) ◽  
pp. 3409-3426
Author(s):  
Arancha Catalan-Moreno ◽  
Marta Cela ◽  
Pilar Menendez-Gil ◽  
Naiara Irurzun ◽  
Carlos J Caballero ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Rna Structure ◽  
Cold Shock ◽  
Mrna Translation ◽  
Site Directed Mutagenesis ◽  
Rna Structures ◽  
Double Stranded Rna ◽  
Ambient Temperatures ◽  
Shock Proteins ◽  
Rna Hairpin

Abstract Thermoregulation of virulence genes in bacterial pathogens is essential for environment-to-host transition. However, the mechanisms governing cold adaptation when outside the host remain poorly understood. Here, we found that the production of cold shock proteins CspB and CspC from Staphylococcus aureus is controlled by two paralogous RNA thermoswitches. Through in silico prediction, enzymatic probing and site-directed mutagenesis, we demonstrated that cspB and cspC 5′UTRs adopt alternative RNA structures that shift from one another upon temperature shifts. The open (O) conformation that facilitates mRNA translation is favoured at ambient temperatures (22°C). Conversely, the alternative locked (L) conformation, where the ribosome binding site (RBS) is sequestered in a double-stranded RNA structure, is folded at host-related temperatures (37°C). These structural rearrangements depend on a long RNA hairpin found in the O conformation that sequesters the anti-RBS sequence. Notably, the remaining S. aureus CSP, CspA, may interact with a UUUGUUU motif located in the loop of this long hairpin and favour the folding of the L conformation. This folding represses CspB and CspC production at 37°C. Simultaneous deletion of the cspB/cspC genes or their RNA thermoswitches significantly decreases S. aureus growth rate at ambient temperatures, highlighting the importance of CspB/CspC thermoregulation when S. aureus transitions from the host to the environment.

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