Structural and Calorimetric Studies Demonstrate that Xeroderma Pigmentosum Type G (XPG) Can Be Imported to the Nucleus by a Classical Nuclear Import Pathway via a Monopartite NLS Sequence
详细信息 查看全文
- 作者：Andrea C. de Barros1 ; Agnes A.S. Takeda1 ; Thiago R. Dreyer1 ; Adrian Velazquez-Campoy2 ; 3 ; 4 ; Bostjan Kobe5 ; Marcos R.M. Fontes1 ; fontes@ibb.unesp.br" class="auth_mail" title="E-mail the corresponding author
- 关键词：importin-α ; xeroderma pigmentosum protein ; nuclear localization sequence (NLS) ; DNA repair proteins ; nucleotide excision repair
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：22 May 2016
- 年：2016
- 卷：428
- 期：10
- 页码：2120-2131
- 全文大小：1391 K
文摘
- •
Structures of importin‐α and putative NLS peptides of the XPG protein were solved.
- •
ITC assays with putative NLS peptides (XPG1 and XPG2) and Importin‐α were performed.
- •
Unexpectedly, both putative peptides bind to Importin‐α as monopartite NLSs.
- •
XPG1 NLS fragment is able to bind with high affinity to Importin‐α receptor.
- •
XPG2 NLS fragment may represent a nuclear retention signal instead of an NLS.