Analysis of interactions and prion transmission between yeast proteins with different homology levels

Anastasia V. Grizel, Aleksandr A. Rubel, Sergey P. Varchenko, Stanislav A. Bondarev, Andrey V. Kajava, Yury O. Chernoff

Результат исследований: Научные публикации в периодических изданияхтезисы

Выдержка

Prions are self-perpetuating aggregated proteins associated with fatal diseases in mammals and controlling heritable traits in yeast. Transmission of mammalian prions between different species is usually impaired, due differences in the primary structures of prion-forming proteins. However, this barrier could be overcome, for example in case of ‘mad cow’ disease transmission to humans. Interspecies transmission barriers were also shown for yeast prions. We used a yeast Sup35/[PSI+] experimental system to explore prion transmission barriers, and studied Sup35 proteins from four yeast species that show from 90 to 60% of amino acid similarity in their NM regions including prion domains, namely Saccharomyces cerevisiae, S. paradoxus, S. bayanus and Lachancea kluyveri. In contrast to previous work where specific prion isolates were tested, we induced prions by overproducing a divergent protein, that produces multiple prion variants. Only the most closely related Sup35NM region from S. paradoxus (90% identity) cou
Язык оригиналаанглийский
Число страниц1
ЖурналYeast
Том32
СостояниеОпубликовано - 2015

Отпечаток

Fungal Proteins
Prions
Yeast
Proteins
Yeasts
Bovine Spongiform Encephalopathy
Mammals
Saccharomyces cerevisiae
Amino acids
Amino Acids

Цитировать

Grizel, Anastasia V. ; Rubel, Aleksandr A. ; Varchenko, Sergey P. ; Bondarev, Stanislav A. ; Kajava, Andrey V. ; Chernoff, Yury O. / Analysis of interactions and prion transmission between yeast proteins with different homology levels. В: Yeast. 2015 ; Том 32.
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title = "Analysis of interactions and prion transmission between yeast proteins with different homology levels",
abstract = "Prions are self-perpetuating aggregated proteins associated with fatal diseases in mammals and controlling heritable traits in yeast. Transmission of mammalian prions between different species is usually impaired, due differences in the primary structures of prion-forming proteins. However, this barrier could be overcome, for example in case of ‘mad cow’ disease transmission to humans. Interspecies transmission barriers were also shown for yeast prions. We used a yeast Sup35/[PSI+] experimental system to explore prion transmission barriers, and studied Sup35 proteins from four yeast species that show from 90 to 60{\%} of amino acid similarity in their NM regions including prion domains, namely Saccharomyces cerevisiae, S. paradoxus, S. bayanus and Lachancea kluyveri. In contrast to previous work where specific prion isolates were tested, we induced prions by overproducing a divergent protein, that produces multiple prion variants. Only the most closely related Sup35NM region from S. paradoxus (90{\%} identity) cou",
author = "Grizel, {Anastasia V.} and Rubel, {Aleksandr A.} and Varchenko, {Sergey P.} and Bondarev, {Stanislav A.} and Kajava, {Andrey V.} and Chernoff, {Yury O.}",
year = "2015",
language = "English",
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journal = "Yeast",
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Analysis of interactions and prion transmission between yeast proteins with different homology levels. / Grizel, Anastasia V.; Rubel, Aleksandr A.; Varchenko, Sergey P.; Bondarev, Stanislav A.; Kajava, Andrey V.; Chernoff, Yury O.

В: Yeast, Том 32, 2015.

Результат исследований: Научные публикации в периодических изданияхтезисы

TY - JOUR

T1 - Analysis of interactions and prion transmission between yeast proteins with different homology levels

AU - Grizel, Anastasia V.

AU - Rubel, Aleksandr A.

AU - Varchenko, Sergey P.

AU - Bondarev, Stanislav A.

AU - Kajava, Andrey V.

AU - Chernoff, Yury O.

PY - 2015

Y1 - 2015

N2 - Prions are self-perpetuating aggregated proteins associated with fatal diseases in mammals and controlling heritable traits in yeast. Transmission of mammalian prions between different species is usually impaired, due differences in the primary structures of prion-forming proteins. However, this barrier could be overcome, for example in case of ‘mad cow’ disease transmission to humans. Interspecies transmission barriers were also shown for yeast prions. We used a yeast Sup35/[PSI+] experimental system to explore prion transmission barriers, and studied Sup35 proteins from four yeast species that show from 90 to 60% of amino acid similarity in their NM regions including prion domains, namely Saccharomyces cerevisiae, S. paradoxus, S. bayanus and Lachancea kluyveri. In contrast to previous work where specific prion isolates were tested, we induced prions by overproducing a divergent protein, that produces multiple prion variants. Only the most closely related Sup35NM region from S. paradoxus (90% identity) cou

AB - Prions are self-perpetuating aggregated proteins associated with fatal diseases in mammals and controlling heritable traits in yeast. Transmission of mammalian prions between different species is usually impaired, due differences in the primary structures of prion-forming proteins. However, this barrier could be overcome, for example in case of ‘mad cow’ disease transmission to humans. Interspecies transmission barriers were also shown for yeast prions. We used a yeast Sup35/[PSI+] experimental system to explore prion transmission barriers, and studied Sup35 proteins from four yeast species that show from 90 to 60% of amino acid similarity in their NM regions including prion domains, namely Saccharomyces cerevisiae, S. paradoxus, S. bayanus and Lachancea kluyveri. In contrast to previous work where specific prion isolates were tested, we induced prions by overproducing a divergent protein, that produces multiple prion variants. Only the most closely related Sup35NM region from S. paradoxus (90% identity) cou

M3 - Meeting Abstract

VL - 32

JO - Yeast

JF - Yeast

SN - 0749-503X

ER -