Dataset Information

Identification of full length Hsp90 from Giardia lamblia cell lysate

ABSTRACT: In the present study using mass-spectrometry we identify the sequence of the unique, junctional peptide contributed by the 5’ UTR of HspC ORF in the full length Hsp90 from Giardia lamblia. This peptide is critical for the catalytic function of Hsp90 as it harbours an essential “Arg” homolog in its sequence. We also show that full length GlHsp90 possesses all the functional hall marks of a canonical Hsp90 including its ability to bind and hydrolyze ATP.

INSTRUMENT(S):

ORGANISM(S): Giardia Lamblia Atcc 50803

TISSUE(S): Trophozoite

DISEASE(S): Giardiasis

SUBMITTER: Utpal Tatu

LAB HEAD: Prof. Utpal Tatu

PROVIDER: PXD000795 | Pride | 2016-07-09

REPOSITORIES: Pride

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Publications

Trans-spliced heat shock protein 90 modulates encystation in Giardia lamblia.

Nageshan Rishi Kumar RK Roy Nainita N Ranade Shatakshi S Tatu Utpal U

PLoS neglected tropical diseases 20140501 5

<h4>Background</h4>Hsp90 from Giardia lamblia is expressed by splicing of two independently transcribed RNA molecules, coded by genes named HspN and HspC located 777 kb apart. The reasons underlying such unique trans-splicing based generation of GlHsp90 remain unclear.<h4>Principle finding</h4>In this study using mass-spectrometry we identify the sequence of the unique, junctional peptide contributed by the 5' UTR of HspC ORF. This peptide is critical for the catalytic function of Hsp90 as it ha ...[more]

PMID: 24786776

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	RAW.wiff	Wiff
	RAW.wiff.scan	Wiff
	SEARCH.xml	Xml
	SEARCHwithflhsp90.xml	Xml

Dataset Information

Identification of full length Hsp90 from Giardia lamblia cell lysate

Dataset's files

Publications

Trans-spliced heat shock protein 90 modulates encystation in Giardia lamblia.

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