ORCID Profile
0000-0001-5851-7692
Current Organisation
Earlham Institute
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Publisher: Cold Spring Harbor Laboratory
Date: 17-12-2022
DOI: 10.1101/2022.12.16.520718
Abstract: The genetic code is one of the most highly conserved features across life. Only a few lineages have deviated from the “universal” genetic code. Amongst the few variants of the genetic code reported to date, the codons UAA and UAG virtually always have the same translation, suggesting that their evolution is coupled. Here, we report the genome and transcriptome sequencing of a novel ciliate, belonging to the Oligohymenophorea class, where the translation of the UAA and UAG stop codons have changed to specify different amino acids. Genomic and transcriptomic analyses revealed that UAA has been reassigned to encode lysine, while UAG has been reassigned to encode glutamic acid. We identified multiple suppressor tRNA genes with anticodons complementary to the reassigned codons. We show that the retained UGA stop codon is enriched in the 3’UTR immediately downstream of the coding region of genes, suggesting that there is functional drive to maintain tandem stop codons. Using a phylogenomics approach, we reconstructed the ciliate phylogeny and mapped genetic code changes, highlighting the remarkable number of independent genetic code changes within the Ciliophora group of protists. According to our knowledge, this is the first report of a genetic code variant where UAA and UAG encode different amino acids.
Publisher: American Society for Microbiology
Date: 24-02-2021
Abstract: Trichomoniasis, caused by the protozoan Trichomonas vaginalis , is the most common nonviral sexually transmitted infection in humans. The millions of cases each year have sequelae that may include complications during pregnancy and increased risk of HIV infection.
Publisher: Springer Science and Business Media LLC
Date: 24-04-2014
Publisher: Elsevier BV
Date: 2013
Publisher: Springer Science and Business Media LLC
Date: 03-02-2023
Publisher: American Society for Microbiology
Date: 11-2014
DOI: 10.1128/EC.00027-14
Abstract: Mutations in the Plasmodium falciparum chloroquine resistance transporter ( Pf CRT) protein confer resistance to the antimalarial drug chloroquine. Pf CRT localizes to the parasite digestive vacuole, the site of chloroquine action, where it mediates resistance by transporting chloroquine out of the digestive vacuole. Pf CRT belongs to a family of transporter proteins called the chloroquine resistance transporter family. CRT family proteins are found throughout the Apicomplexa, in some protists, and in plants. Despite the importance of Pf CRT in drug resistance, little is known about the evolution or native function of CRT proteins. The apicomplexan parasite Toxoplasma gondii contains one CRT family protein. We demonstrate that T. gondii CRT ( Tg CRT) colocalizes with markers for the vacuolar (VAC) compartment in these parasites. The Tg CRT-containing VAC is a highly dynamic organelle, changing its morphology and protein composition between intracellular and extracellular forms of the parasite. Regulated knockdown of Tg CRT expression resulted in modest reduction in parasite fitness and swelling of the VAC, indicating that Tg CRT contributes to parasite growth and VAC physiology. Together, our findings provide new information on the role of CRT family proteins in apicomplexan parasites.
Publisher: Oxford University Press (OUP)
Date: 06-2017
DOI: 10.1093/GBE/EVX110
Publisher: Wiley
Date: 19-01-2020
DOI: 10.1111/JEU.12837
Location: United Kingdom of Great Britain and Northern Ireland
Location: United States of America
No related grants have been discovered for Sally Warring.