Optimizing purification of the peripheral membrane protein FAM92A1 fused to a modified spidroin tag

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Fältnamn	Indikatorer	Metadata
000		03009naa a2200349 4500
001		oai:DiVA.org:kth-304498
003		SwePub
008		211104s2022 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3044982 URI
024	7	a https://doi.org/10.1016/j.pep.2021.1059922 DOI
040		a (SwePub)kth
041		a engb eng
042		9 SwePub
072	7	a vet2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Wang, Zuoneng,d 1991-u KTH,Strukturell bioteknik,Carsten Mim4 aut0 (Swepub:kth)u1jskro6
245	1 0	a Optimizing purification of the peripheral membrane protein FAM92A1 fused to a modified spidroin tag
264	1	b Elsevier,c 2022
338		a print2 rdacarrier
500		a QC 20220308
520		a Cryo-electron microscopy has revolutionized structural biology. In particular structures of proteins at themembrane interface have been a major contribution of cryoEM. Yet, visualization and characterization of peripheralmembrane proteins remains challenging; mostly because there is no unified purification strategy forthese proteins. FAM92A1 is a novel peripheral membrane protein that binds to the mitochondrial inner membrane.There, FAM92A1 dimers bind to the membrane and play an essential role in regulating the mitochondrialultrastructure. Curiously, FAM92A1 has also an important function in ciliogenesis. FAM92A1 is part of themembrane bending Bin1/Amphiphsyin/RVS (BAR) domain protein family. Currently, there is no structure ofFAM92A1, mostly because FAM92A1 is unstable and insoluble at high concentrations, like many BAR domainproteins. Yet, pure and concentrated protein is a necessity for screening to generate samples suitable for structuredetermination. Here, we present an optimized purification and expression strategy for dimeric FAM92A1. To ourknowledge, we are the first to use the spidroin tag NT* to successfully purify a peripheral membrane protein. Ourresults show that NT* not only increases solubility but stabilizes FAM92A1 as a dimer. FAM92A1 fused to NT* isactive because it is able to efficiently bend membranes. Taken together, our strategy indicates that this is apossible avenue to express and purify other challenging BAR domain proteins.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653		a Biotechnology
653		a Bioteknologi
653		a Biotechnology
700	1	a Mim, Carstenu KTH,Strukturell bioteknik4 aut0 (Swepub:kth)u1ce0qjf
710	2	a KTHb Strukturell bioteknik4 org
773	0	t Protein Expression and Purificationd : Elsevierg 189, s. 105992-105992q 189<105992-105992x 1046-5928x 1096-0279
856	4	u http://kth.diva-portal.org/smash/get/diva2:1608908/FULLTEXT02
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-304498
856	4 8	u https://doi.org/10.1016/j.pep.2021.105992

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