Yeast Trk1 Potassium Transporter Gradually Changes Its Affinity in Response to Both External and Internal Signals

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F22%3A00557979" target="_blank" >RIV/67985823:_____/22:00557979 - isvavai.cz</a>

Result on the web

<a href="https://www.mdpi.com/2309-608X/8/5/432" target="_blank" >https://www.mdpi.com/2309-608X/8/5/432</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/jof8050432" target="_blank" >10.3390/jof8050432</a>

Result language

angličtina

Original language name

Yeast Trk1 Potassium Transporter Gradually Changes Its Affinity in Response to Both External and Internal Signals

Original language description

Yeasts need a high intracellular concentration of potassium to grow. The main K+ uptake system in Saccharomyces cerevisiae is the Trk1 transporter, a complex protein with four MPM helical membrane motifs. Trk1 has been shown to exist in low- or high-affinity modes, which reflect the availability of potassium in the environment. However, when and how the affinity changes, and whether the potassium availability is the only signal for the affinity switch, remains unknown. Here, we characterize the Trk1 kinetic parameters under various conditions and find that Trk1's K-T and V-max change gradually. This gliding adjustment is rapid and precisely reflects the changes in the intracellular potassium content and membrane potential. A detailed characterization of the specific mutations in the P-helices of the MPM segments reveals that the presence of proline in the P-helix of the second and third MPM domain (F820P and L949P) does not affect the function of Trk1 in general, but rather specifically prevents the transporter's transition to a high-affinity state. The analogous mutations in the two remaining MPM domains (L81P and L1115P) result in a mislocalized and inactive protein, highlighting the importance of the first and fourth P-helices in proper Trk1 folding and activity at the plasma membrane.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

<a href="/en/project/GA20-04420S" target="_blank" >GA20-04420S: Trk1 potassium importers - key transport systems for yeast cell fitness and multiple-stress tolerance</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Fungi

ISSN

2309-608X

e-ISSN

2309-608X

Volume of the periodical

8

Issue of the periodical within the volume

5

Country of publishing house

CH - SWITZERLAND

Number of pages

22

Pages from-to

432

UT code for WoS article

000801269000001

EID of the result in the Scopus database

2-s2.0-85129760926