Proteomics

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Effects of a phosphomimetic mutation and nucleotide binding on the interaction of Hsp90a with co-chaperone Aha1 analyzed by chemical cross-linking with mass spectrometry

ABSTRACT: Complex conformational dynamics are essential for the chaperone function of heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization establishing ATPase competence. Biochemical data demonstrate that the intrinsic, but weak, ATP hydrolyzing activity of Hsp90 is markedly enhanced by the co-chaperone Aha1. However, cellular concentration of Aha1 is substoichiometric relative to Hsp90. In cells, interaction of this important co-chaperone with Hsp90 is up-regulated by posttranslational modifications (PTMs), including phosphorylation of a highly conserved tyrosine (Y313 in Hsp90a). Here we use chemical cross-linking with mass spectrometry to explore the the impacts of a phosphomimetic mutation (Y313E) and binding of a non-hydrolyzable ATP analog (AMP-PNP),on the structure Hsp90a and its interaction with Aha1.

INSTRUMENT(S): LTQ FT, Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Juan Chavez  

LAB HEAD: Len Neckers

PROVIDER: PXD013476 | Pride | 2019-06-17

REPOSITORIES: Pride

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Dataset's files

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Action DRS
071516_Hsp90a_WT_Aha1_AMPPNP_BDP_2hr1.mzXML Mzxml
071516_Hsp90a_WT_Aha1_AMPPNP_BDP_2hr1.pep.xml Pepxml
071516_Hsp90a_WT_Aha1_AMPPNP_BDP_2hr1.pep.xml.react1.xls Pepxml
071516_Hsp90a_WT_Aha1_AMPPNP_BDP_2hr1.pep.xml.react2.xls Pepxml
071516_Hsp90a_WT_Aha1_AMPPNP_BDP_2hr1.raw Raw
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Publications

Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1.

Xu Wanping W   Beebe Kristin K   Chavez Juan D JD   Boysen Marta M   Lu YinYing Y   Zuehlke Abbey D AD   Keramisanou Dimitra D   Trepel Jane B JB   Prodromou Christosomos C   Mayer Matthias P MP   Bruce James E JE   Gelis Ioannis I   Neckers Len L  

Nature communications 20190612 1

Complex conformational dynamics are essential for function of the dimeric molecular chaperone heat shock protein 90 (Hsp90), including transient, ATP-biased N-domain dimerization that is necessary to attain ATPase competence. The intrinsic, but weak, ATP hydrolyzing activity of human Hsp90 is markedly enhanced by the co-chaperone Aha1. However, the cellular concentration of Aha1 is substoichiometric relative to Hsp90. Here we report that initial recruitment of this cochaperone to Hsp90 is marked  ...[more]

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