Isolation and characterisation of a calnexin homologue, clxA, from Aspergillus niger

被引:0
作者
H. Wang
J. Entwistle
E. Morlon
D. B. Archer
J. F. Peberdy
M. Ward
D. J. Jeenes
机构
[1] Genencor International Inc.,Dept. of Food Safety Sciences
[2] Institute of Food Research,School of Life and Environmental Sciences
[3] Nottingham University,undefined
来源
Molecular Genetics and Genomics | 2003年 / 268卷
关键词
Calnexin; Unfolded protein response; Chaperone; Protein folding;
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摘要
We describe the isolation of a gene ( clxA) encoding calnexin from laboratory and industrial strains of Aspergillus niger. Calnexin is a chaperone, which specifically recognises monoglucosylated glycoproteins in the endoplasmic reticulum, and is thus an essential component of the process that assesses the folded state of nascent secreted glycoproteins. Manipulation of chaperones has previously been adopted in attempts to overcome some of the problems associated with the secretion of heterologous proteins from filamentous fungi. The A. niger clxA gene encodes a 562-residue protein with strong homology to the calnexin of Schizosaccharomyces pombe. The clxA gene product complements a S. pombe cnx1 mutant. Motifs associated with genes controlled via the Unfolded Protein Response (UPR) were identified by sequence homology in the promoter of clxA. Steady-state levels of clxA mRNA were elevated in a strain expressing bovine prochymosin fused to the catalytic domain of glucoamylase. The ORF is punctuated by four introns, and contains two sets of four repeated peptide motifs that are characteristic of the calnexin family, together with a putative membrane-spanning domain. Deletion studies indicate that clxA is not an essential gene in A. niger.
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页码:684 / 691
页数:7
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