Single-molecule fret study on structural dynamics of membrane proteins

Atieh Aminian Jazi

doi:10.33612/diss.135802718

Single-molecule fret study on structural dynamics of membrane proteins

Atieh Aminian Jazi

Single-molecule biophysics

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De Na+ -gekoppelde betaïne symporter BetP van de bacterie Corynebacterium glutamicum gaat hyperosmotische stress tegen en wordt gereguleerd via een osmodetecterend C-terminaal domein. Hoewel de biochemie van het systeem goed is gekarakteriseerd, is structurele informatie slechts gedeeltelijk beschikbaar, vanwege een ontbrekend C-terminaal domein in de kristalstructuur. Dus zowel het activerings- als transportmechanisme blijven onopgelost. We hebben verschillende enkele molecuul technieken ontwikkeld om de conformationele dynamiek en heterogeniteit van BetP te bestuderen in proof-of-principle studies en een gedetailleerde mechanistische studie van transportactivatie.

Originele taal-2	English
Kwalificatie	Doctor of Philosophy
Toekennende instantie	Rijksuniversiteit Groningen
Begeleider(s)/adviseur	Cordes, Thorben, Supervisor Poolman, Berend, Supervisor Gkouridis, Giorgios, Co-supervisor
Datum van toekenning	2-jun.-2020
Plaats van publicatie	[Groningen]
Uitgever	University of Groningen
Gedrukte ISBN's	978-90-830-7040-7
DOI's	https://doi.org/10.33612/diss.135802718
Status	Published - 2020

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10.33612/diss.135802718

Title and contentsFinal publisher's version, 255 KB
Chapter 1Final publisher's version, 861 KB
Chapter 2Final publisher's version, 1,39 MB
Chapter 3Final publisher's version, 1,79 MB
Chapter 4Final publisher's version, 2,21 MB
Chapter 5Final publisher's version, 291 KB
Complete thesisFinal publisher's version, 5,65 MB
PropositionsFinal publisher's version, 98,9 KB

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@phdthesis{8b97f4a7d10d49a194af0ece88cfbcb3,

title = "Single-molecule fret study on structural dynamics of membrane proteins",

abstract = "The Na+ coupled betaine symporter BetP counteracts hyperosmotic stress and is regulated via an osmosensing C-terminal domain. While the biochemistry of the system is well characterized, structural information is only partially available due to a lacking C-terminal domain in the crystal structure. Thus, both the activation and transport mechanism remain elusive. In this work, we established different single-molecule-based methods to study the conformational dynamics and heterogeneity of BetP in proof-of-principle studies (chapter 2/3) and a detailed mechanistic study of transport activation. Our studies showed that smFRET approach was sussefully adopted for BetP and we obtained the results that was not yet accompolished by standard strucrtal biology teqniques such as crystal structure method. The established methods will pave the way for future single-molecule studies and enhanced mechanistic understanding of the secondary-active transporter BetP in a near-native biochemistry environment.",

author = "{Aminian Jazi}, Atieh",

year = "2020",

doi = "10.33612/diss.135802718",

language = "English",

isbn = "978-90-830-7040-7",

series = "Zernike Institute for Advanced Materials PhD thesis series",

publisher = "University of Groningen",

number = "14",

school = "University of Groningen",

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T1 - Single-molecule fret study on structural dynamics of membrane proteins

AU - Aminian Jazi, Atieh

PY - 2020

Y1 - 2020

N2 - The Na+ coupled betaine symporter BetP counteracts hyperosmotic stress and is regulated via an osmosensing C-terminal domain. While the biochemistry of the system is well characterized, structural information is only partially available due to a lacking C-terminal domain in the crystal structure. Thus, both the activation and transport mechanism remain elusive. In this work, we established different single-molecule-based methods to study the conformational dynamics and heterogeneity of BetP in proof-of-principle studies (chapter 2/3) and a detailed mechanistic study of transport activation. Our studies showed that smFRET approach was sussefully adopted for BetP and we obtained the results that was not yet accompolished by standard strucrtal biology teqniques such as crystal structure method. The established methods will pave the way for future single-molecule studies and enhanced mechanistic understanding of the secondary-active transporter BetP in a near-native biochemistry environment.

AB - The Na+ coupled betaine symporter BetP counteracts hyperosmotic stress and is regulated via an osmosensing C-terminal domain. While the biochemistry of the system is well characterized, structural information is only partially available due to a lacking C-terminal domain in the crystal structure. Thus, both the activation and transport mechanism remain elusive. In this work, we established different single-molecule-based methods to study the conformational dynamics and heterogeneity of BetP in proof-of-principle studies (chapter 2/3) and a detailed mechanistic study of transport activation. Our studies showed that smFRET approach was sussefully adopted for BetP and we obtained the results that was not yet accompolished by standard strucrtal biology teqniques such as crystal structure method. The established methods will pave the way for future single-molecule studies and enhanced mechanistic understanding of the secondary-active transporter BetP in a near-native biochemistry environment.

U2 - 10.33612/diss.135802718

DO - 10.33612/diss.135802718

M3 - Thesis fully internal (DIV)

SN - 978-90-830-7040-7

T3 - Zernike Institute for Advanced Materials PhD thesis series

PB - University of Groningen

CY - [Groningen]

ER -

Single-molecule fret study on structural dynamics of membrane proteins

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