Y-box-binding protein 1 as a non-canonical factor of base excision repair

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Y-box-binding protein 1 as a non-canonical factor of base excision repair

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作者：Elizaveta E. Alemasova^a ; Nina A. Moor^a ; ^b ; Konstantin N. Naumenko^a ; ^b ; Mikhail M. Kutuzov^a ; Maria V. Sukhanova^a ; ^b ; Pavel E. Pestryakov^a ; Olga I. Lavrik^a ; ^b ; ^{lavrik@niboch.nsc.ru" class="auth_mail" title="E-mail the corresponding author}
关键词：YB-1 ; Y-box binding protein 1 ; PARP1(2) ; poly(ADP-ribose) polymerase 1(2) ; PAR ; poly(ADP-ribose) ; PARG ; poly(ADP-ribose) glycohydrolase ; pol β ; DNA polymerase beta ; APE1 ; AP endonuclease 1 ; NEIL1 ; Nei-like DNA glycosylase 1 ; AP site ; apurinic/apyrimidinic ; abasic site ; BER ; base excision repair
刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
出版年：2016
出版时间：December 2016
年：2016
卷：1864
期：12
页码：1631-1640
全文大小：963 K

文摘

•: YB-1 and its nuclear form physically interact with key BER factors.
•: YB-1 interaction with PARP1 DNA-binding domain is modulated by DNA.
•: Poly(ADP-ribosyl)ation of YB-1 can be activated by RNA.
•: YB-1 is able to stimulate PARP1 activity and to increase the life span of PAR polymer.
•: YB-1 can modulate NEIL1 and Pol β lyase activities.

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