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UID:918@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20200908T130000

DTEND;TZID=Asia/Jerusalem:20200908T140000

DTSTAMP:20210802T125902Z

URL:https://biology.technion.ac.il/en/seminars/m-sc-graduate-seminar-maria
 n-nicola-2/

SUMMARY:M.Sc. Graduate Seminar-Marian Nicola [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n The RNA recognition moti
 f (RRM) is found approximately in all lifekingdoms and is one of the most 
 abundant protein domains. RRM-containingproteins take part in post transcr
 iptional events such as: pre-mRNA processing\,splicing\, alternative splic
 ing\, mRNA stability\, mRNA export\, RNA editing\, andtranslation regulati
 on. My M.Sc. project focuses on RNA-binding motif 42(RBM42) that contains 
 one RRM motif at its C-terminal region. Unpublished workfrom our lab impli
 cated RBM42 in RNA splicing and DNA damage response (DDR) bya yet unknown 
 mechanism. In an attempt to shed molecular insights into how RBM42regulate
 s splicing and DNA repair\, we sought to map RBM42 interactome using ascor
 bateperoxidase (APEX2)-based proximity labelling approach combined with Ma
 ssSpectrometry. Toward this end\, we used CRISPR-cas9 methodology to knock
 -inAPEX2 to the C-terminal of the endogenous RBM42. RBM42 proximal protein
 s werebiotinylated by APEX2 activation using H2O2 and subjectedto Mass spe
 ctrometry. Interactome analysis substantiates RBM42 role in mRNA splicing 
 andDNA damage repair and revealed unexpected pathways that are regulated b
 y RBM42such as protein synthesis. During the seminar\, I will elaborate on
  how RBM42interactome advances our understanding of RBM42 biological funct
 ions. 

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