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UID:921@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20201024T231500

DTEND;TZID=Asia/Jerusalem:20201025T001500

DTSTAMP:20210802T125902Z

URL:https://biology.technion.ac.il/en/seminars/m-sc-graduate-seminar-manis
 ha-sahoo-2/

SUMMARY:M.Sc. Graduate Seminar-Manisha Sahoo [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n Manisha SahooFrom the La
 b of Doctor Kleifeld OdedResearch Topic:  Proteomic profiling of active
 proteasomes and intracellular peptidome The proteasomes are multisubunit\,
 multicatalytic protein complex in eukaryotic cells which degrade misfolded
 \,damaged\, or unstructured proteins. Functionally it is divided into a 20
 Scatalytic core particle and two 19S regulatory particles at both side of 
 20Sparticle.  In eukaryotic cells activeproteasomes exist inthree major t
 ypes:doubly capped proteasomes - 30S (two 19S on both side of 20S)\, singl
 y cappedproteasomes – 26S (one 19S on 20S) and 20S proteasomes. The19S r
 ecognizes and binds ubiquitin modified target proteins to be degraded bypr
 oteasomes. Then after gets unfolded\, the target protein is catalyticallyc
 leaved inside the 20S core and released as peptide products. Thecompositio
 n and amount of each of the proteasome active forms are dynamicallycontrol
 led by the cellular conditions and thought to be directed towardsdifferent
  types of substrates and to generate different types of products.Unlike th
 e lysosome\, where proteases shear proteins up into individual aminoacids\
 , the proteasome just chops proteins into small peptides\, with an mean av
 eragesize of 10-12 amino acids length.These peptides can further be proces
 sedto single amino acids or possibly be used in many cellular signaling pa
 thways. Thecurrent study is based on to develop a methodology  for profil
 ing of active proteasome and  the analysis of peptidome generated bydiffe
 rent types of proteasomes in yeast cellular system.  

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