PXD038235-1

PXD038235 is an original dataset announced via ProteomeXchange.

Title	Proteomic analysis defines the interactome of telomerase in the protozoan parasite, Trypanosoma brucei
Description	Telomeres are the nucleoprotein structures found at the ends of eukaryotic chromosomes. Conventional DNA polymerases are unable to fully replicate the telomeric end of the chromosome, which leads to a progressive loss of DNA after every cell division. This problem is solved by the ribonucleoprotein enzyme, telomerase. Proper maintenance of the telomeric end is critical for maintaining genome integrity in eukaryotes. The telomerase enzyme has two essential components: the telomerase RNA (TR), which provides the template required for telomeric DNA synthesis; and the catalytic protein telomerase reverse transcriptase (TERT) that catalyzes the extension of the telomeric DNA ends using the TR as a template. The action of telomerase prevents the progressive shortening of the telomeres after every cell division. The TR can form a large structural scaffold upon which many accessory proteins can bind to and form the complete telomerase holoenzyme in vivo. These accessory proteins are required for telomerase activity and regulation inside of cells. The interacting partners of the TERT protein have been extensively characterized in yeast, human, and Tetrahymena systems. These interactors have not been extensively studied in lower eukaryotes including clinically relevant human parasites, such as Trypanosoma brucei (T. brucei). To this end, we performed co-immunoprecipitation coupled to LC-MS/MS of TbTERT-FLAG-HA-HA from T. brucei cells using an anti-TbTERT antibody and protein G magnetic beads. An isotype matched IgG control was performed in tandem. Comparisons of enriched proteins in the IP vs. IgG control revealed previously known and novel interactors of TbTERT. These findings suggest potential mechanistic differences in telomere maintenance in T. brucei compared to higher eukaryotes.
HostingRepository	PRIDE
AnnounceDate	2023-03-08
AnnouncementXML	Submission_2023-03-08_11:44:34.335.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	ShoulingXu
SpeciesList	scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-21 16:10:48	ID requested
⏵ 1	2023-03-08 11:44:34	announced

Dataset with its publication pending

submitter keyword: co-immunoprecipitation, telomerase, interaction partners,Trypanosoma brucei, telomerase RNA, LC-MS/MS

ShoulingXu
contact affiliation	Carnegie Mass Spectrometry Facility
contact email	sxu@ciw.edu
lab head
ShoulingXu
contact affiliation	Carnegie Institution at Stanford
contact email	sxu@ciw.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD038235
     1. Label: PRIDE project
     2. Name: Proteomic analysis defines the interactome of telomerase in the protozoan parasite, Trypanosoma brucei