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FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa.

作者信息

Tremmel Dirk, Duarte Margarida, Videira Arnaldo, Tropschug Maximilian

机构信息

Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und molekulare Zellforschung, Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.

出版信息

FEBS Lett. 2007 May 15;581(10):2036-40. doi: 10.1016/j.febslet.2007.04.042. Epub 2007 Apr 25.

DOI:10.1016/j.febslet.2007.04.042
PMID:17470367
Abstract

FKBP22 is a dimeric protein in the lumen of the endoplasmic reticulum, which exhibits a chaperone as well as a PPIase activity. It binds via its FK506 binding protein (FKBP) domain directly to the Hsp70 chaperone BiP that stimulates the chaperone activity of FKBP22. Here we demonstrate additionally the association of FKBP22 with the molecular chaperones and folding catalysts Grp170, alpha-subunit of glucosidase II, PDI, ERp38, and CyP23. These proteins are associated with FKBP22 in at least two protein complexes. Furthermore, we report an essential role for FKBP22 in the development of microconidiophores in Neurospora crassa.

摘要

相似文献

1
FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa.
FEBS Lett. 2007 May 15;581(10):2036-40. doi: 10.1016/j.febslet.2007.04.042. Epub 2007 Apr 25.
2
Neurospora crassa FKBP22 is a novel ER chaperone and functionally cooperates with BiP.粗糙脉孢菌FKBP22是一种新型内质网伴侣蛋白，与结合免疫球蛋白蛋白（BiP）在功能上相互协作。
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Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance.利用表面等离子体共振技术对嗜冷FKBP22与蛋白质折叠中间体进行结合分析。
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Role of polar and nonpolar residues at the active site for PPIase activity of FKBP22 from Shewanella sp. SIB1.施氏假单胞菌 FKBP22 的活性位点的极性和非极性残基在 PPIase 活性中的作用。
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Engineering of monomeric FK506-binding protein 22 with peptidyl prolyl cis-trans isomerase. Importance of a V-shaped dimeric structure for binding to protein substrate.具有肽基脯氨酰顺反异构酶活性的单体FK506结合蛋白22的工程改造。V形二聚体结构对与蛋白质底物结合的重要性。
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The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity.FKBP23与BiP的结合通过其肽基脯氨酰顺反异构酶（PPIase）活性调节BiP的ATP酶活性。
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The mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentration.小鼠FKBP23在内质网中与BiP结合，其C末端结构域的结合与Ca2+浓度相关。
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Protein folding and quality control in the endoplasmic reticulum.内质网中的蛋白质折叠与质量控制
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