Trypanosoma brucei Tb927.2.6100 Is an Essential Protein Associated with Kinetoplast DNA

Handle URI:
http://hdl.handle.net/10754/554106
Title:
Trypanosoma brucei Tb927.2.6100 Is an Essential Protein Associated with Kinetoplast DNA
Authors:
Beck, K.; Acestor, N.; Schulfer, A.; Anupama, A.; Carnes, J.; Panigrahi, A. K.; Stuart, K.
Abstract:
The mitochondrial DNA of trypanosomatid protozoa consists of a complex, intercatenated network of tens of maxicircles and thousands of minicircles. This structure, called kinetoplast DNA (kDNA), requires numerous proteins and multiprotein complexes for replication, segregation, and transcription. In this study, we used a proteomic approach to identify proteins that are associated with the kDNA network. We identified a novel protein encoded by Tb927.2.6100 that was present in a fraction enriched for kDNA and colocalized the protein with kDNA by fluorescence microscopy. RNA interference (RNAi) knockdown of its expression resulted in a growth defect and changes in the proportion of kinetoplasts and nuclei in the cell population. RNAi also resulted in shrinkage and loss of the kinetoplasts, loss of maxicircle and minicircle components of kDNA at similar rates, and (perhaps secondarily) loss of edited and pre-edited mRNA. These results indicate that the Tb927.2.6100 protein is essential for the maintenance of kDNA.
KAUST Department:
Biosciences Core Lab
Citation:
Trypanosoma brucei Tb927.2.6100 Is an Essential Protein Associated with Kinetoplast DNA 2013, 12 (7):970 Eukaryotic Cell
Publisher:
American Society for Microbiology
Journal:
Eukaryotic Cell
Issue Date:
6-May-2013
DOI:
10.1128/EC.00352-12
PubMed ID:
23650088
PubMed Central ID:
PMC3697465
Type:
Article
ISSN:
1535-9778; 1535-9786
Additional Links:
http://ec.asm.org/cgi/doi/10.1128/EC.00352-12
Appears in Collections:
Articles; Biosciences Core Lab; Biosciences Core Lab

Full metadata record

DC FieldValue Language
dc.contributor.authorBeck, K.en
dc.contributor.authorAcestor, N.en
dc.contributor.authorSchulfer, A.en
dc.contributor.authorAnupama, A.en
dc.contributor.authorCarnes, J.en
dc.contributor.authorPanigrahi, A. K.en
dc.contributor.authorStuart, K.en
dc.date.accessioned2015-05-18T21:54:04Zen
dc.date.available2015-05-18T21:54:04Zen
dc.date.issued2013-05-06en
dc.identifier.citationTrypanosoma brucei Tb927.2.6100 Is an Essential Protein Associated with Kinetoplast DNA 2013, 12 (7):970 Eukaryotic Cellen
dc.identifier.issn1535-9778en
dc.identifier.issn1535-9786en
dc.identifier.pmid23650088en
dc.identifier.doi10.1128/EC.00352-12en
dc.identifier.urihttp://hdl.handle.net/10754/554106en
dc.description.abstractThe mitochondrial DNA of trypanosomatid protozoa consists of a complex, intercatenated network of tens of maxicircles and thousands of minicircles. This structure, called kinetoplast DNA (kDNA), requires numerous proteins and multiprotein complexes for replication, segregation, and transcription. In this study, we used a proteomic approach to identify proteins that are associated with the kDNA network. We identified a novel protein encoded by Tb927.2.6100 that was present in a fraction enriched for kDNA and colocalized the protein with kDNA by fluorescence microscopy. RNA interference (RNAi) knockdown of its expression resulted in a growth defect and changes in the proportion of kinetoplasts and nuclei in the cell population. RNAi also resulted in shrinkage and loss of the kinetoplasts, loss of maxicircle and minicircle components of kDNA at similar rates, and (perhaps secondarily) loss of edited and pre-edited mRNA. These results indicate that the Tb927.2.6100 protein is essential for the maintenance of kDNA.en
dc.publisherAmerican Society for Microbiologyen
dc.relation.urlhttp://ec.asm.org/cgi/doi/10.1128/EC.00352-12en
dc.rightsArchived with thanks to Eukaryotic Cellen
dc.titleTrypanosoma brucei Tb927.2.6100 Is an Essential Protein Associated with Kinetoplast DNAen
dc.typeArticleen
dc.contributor.departmentBiosciences Core Laben
dc.identifier.journalEukaryotic Cellen
dc.identifier.pmcidPMC3697465en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionSeattle Biomedical Research Institute, Seattle, Washington, USAen
kaust.authorPanigrahi, Aswini Kumaren
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