Proteomics

Dataset Information

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Crosslinking Mapping of yeast Komagataella phaffii TFIID complex

ABSTRACT: Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP-associate factors (Tafs) providing regulatory and chromatin binding functions. We used CXMS to study the organization and structure of the purified TFIID complex from Komagataella phaffii. Together with Cryo-EM, We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a HF domain. Interaction with promoter DNA highlights two non-selective binding sites consistent with a DNA scanning mode.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Komagataella Phaffii

SUBMITTER: Jie Luo  

LAB HEAD: Jeff Ranish

PROVIDER: PXD011092 | Pride | 2018-10-08

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
JL072617_072617_PpTFIID_100B.raw Raw
JL072617_072617_PpTFIID_1ug.raw Raw
JL072617_072617_PpTFIID_30B.raw Raw
JL072617_072617_PpTFIID_50B.raw Raw
JL072617_072617_PpTFIID_70B.raw Raw
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Publications

Microtubule end conversion mediated by motors and diffusing proteins with no intrinsic microtubule end-binding activity.

Chakraborty Manas M   Tarasovetc Ekaterina V EV   Zaytsev Anatoly V AV   Godzi Maxim M   Figueiredo Ana C AC   Ataullakhanov Fazly I FI   Grishchuk Ekaterina L EL  

Nature communications 20190411 1

Accurate chromosome segregation relies on microtubule end conversion, the ill-understood ability of kinetochores to transit from lateral microtubule attachment to durable association with dynamic microtubule plus-ends. The molecular requirements for this conversion and the underlying biophysical mechanisms are elusive. We reconstituted end conversion in vitro using two kinetochore components: the plus end-directed kinesin CENP-E and microtubule-binding Ndc80 complex, combined on the surface of a  ...[more]

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