Ctenopharyngodon idella IKKβ interacts with PKR
and IκBα
Haizhou Wang;Qun Xu;Xiaowen Xu;Yousheng Hu;Qunhao Hou;Youlin Zhu;Chengyu Hu
【期刊名称】《生物化学与生物物理学报:英文版》 【年(卷),期】2017(049)008
【摘要】Inhibitor of nuclear factor kappa-B kinase β (IKKβ) is a subunit of the IKK complex.It can activate the NF-κB pathway through phosphorylating IκB in response to a wide range of stimuli.In the present study,an IKKβ gene from grass carp (Ctenopharyngodon idella;kT282114) was cloned and identified by homologous cloning and rapid-amplification of cDNA ends (RACE) technique.The complete CiIKKβ cDNA is 3428 bp in length,with the longest open reading frame (ORF) of 2337bp encoding a polypeptide of 778 amino acids.The deduced amino acid sequence of CiIKKβ has similar domain distribution to
those
of
mammalian.For
example,CiIKKβ
consists
of
a
serine/threonine kinase domain at the N-terminal,a basic region leucin zipper (BRLZ) domain in the middle,a homeobox associated leucin zipper (HALZ) domain and an IKKβ NEMO (NF-κB essential modulator) binding domain at the C-terminal.Phylogenetic tree analysis also showed that CiIKKβ is highly homologous to zebrafish IKKβ (DrIKKβ) and
clearly
distinct
from
the
mammalian
and
amphibian
counterparts.The expression of CiIKKβ was ubiquitously found in the
Ctenopharyngodon idella IKKβ interacts with PKR and IκBα
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