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Crystal structure of NusG N‐terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE″
Author(s) -
Zhou Huihao,
Liu Qi,
Gao Yongxiang,
Teng Maikun,
Niu Liwen
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22465
Subject(s) - archaea , biology , transcription (linguistics) , transcription factor , eukaryotic transcription , bacteria , computational biology , promoter , genetics , gene , gene expression , linguistics , philosophy
Transcription in archaea employs a eukaryotic‐type transcription apparatus but uses bacterial‐type transcription factors. NusG is one of the few archaeal transcription factors whose orthologs are essential in both bacteria and eukaryotes. Archaeal NusG is composed of only an NusG N‐terminal (NGN) domain and a KOW domain, which is similar to bacterial NusG but not to the eukaryotic ortholog, Spt5. However, archaeal NusG was confirmed recently to form a complex with rpoE″ that was similar to the Spt5‐Spt4 complex. Thus, archaeal NusG presents hybrid features of Spt5 and bacterial NusG. Here we report the crystal structure of NGN from the archaea Methanocaldococcus jannaschii ( Mj NGN). Mj NGN folds to an α‐β‐α sandwich without the appendant domain of bacterial NGNs, and forms a unique homodimer in crystal and solution. Mj NGN alone was found to be sufficient for rpoE″ binding and an Mj NGN‐rpoE″ model has been constructed by rigid docking. Proteins 2009. © 2009 Wiley‐Liss, Inc.