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UID:1166@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20230321T130000

DTEND;TZID=Asia/Jerusalem:20230321T140000

DTSTAMP:20230316T070946Z

URL:https://biology.technion.ac.il/en/seminars/phd-graduate-seminar-layla-
 saied/

SUMMARY:PhD Graduate Seminar- Layla Saied [No Categories]
DESCRIPTION:Location: hybrid- in the Faculty Auditorium/ZOOM: https://techn
 ion.zoom.us/https://technion.zoom.us/j/98681053470?pwd=Tk1lR3pqOTdEMy9oQW8
 zbFFDOUxoUT09  Layla Saied\n Affiliation: \n Host:Dr. Kleifeld Oded \n Cha
 racterization of Peroxismoal Proteins Changes in Response to Stress\n\n&nb
 sp\;\n\nPeroxisomes are organelles with a single bilayer membrane that enc
 loses a soluble matrix space. Their importance is highlighted by the sever
 e inherited diseases that result from impairments in one or more peroxisom
 al functions. These organelles are highly diverse and can contain various 
 sets of enzymes. Most types of peroxisomes are involved in beta-oxidation 
 of fatty acids and maintaining reactive oxygen species homeostasis. Peroxi
 somes can adapt to different functions by importing different proteins and
  enzymes.\n\nProper functionality of this organelle requires specific qual
 ity control. One of the enzymes that have an important role in maintaining
  the peroxisome homeostasis and functionality is the peroxisomal isoform L
 on peptidase 2 (LonP2). The enzyme has both a chaperone activity and prote
 olytic activity. However\, not a lot is known about the function of this L
 on protease isoform.\n\nI will present a new method developed to study the
  peroxisomal import machinery and the results obtained from it. Additional
 ly\, I will outline the results obtained through various cellular\, bioche
 mical\, and proteomics approaches regarding the role of LonP2.\n\n&nbsp\;\
 n\n&nbsp\; 
LOCATION:hybrid- in the Faculty Auditorium/ZOOM: https://technion.zoom.us/h
 ttps://technion.zoom.us/j/98681053470?pwd=Tk1lR3pqOTdEMy9oQW8zbFFDOUxoUT09

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