The SEA complex – the beginning
Наличие разнообразных внутриклеточных мембранных органелл, динамически связанных посредством селективного транспорта, является отличительной особенностью эукариотической клетки. Множество белков, необходимых для образования и существования этих органелл, имеют сходную эволюционную историю. Недавно м...
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Algret R. Dokudovskaya, S.S. 2019-06-19T10:54:08Z 2019-06-19T10:54:08Z 2012 The SEA complex – the beginning / R.Algret, S.S. Dokudovskaya // Вiopolymers and Cell. — 2012. — Т. 28, № 4. — С. 281–284. — Бібліогр.: 20 назв. — англ. 0233-7657 DOI: http://dx.doi.org/10.7124/bc.00005A https://nasplib.isofts.kiev.ua/handle/123456789/156925 577.22 Наличие разнообразных внутриклеточных мембранных органелл, динамически связанных посредством селективного транспорта, является отличительной особенностью эукариотической клетки. Множество белков, необходимых для образования и существования этих органелл, имеют сходную эволюционную историю. Недавно мы открыли новый консервативный белковый комплекс – SEA-комплекс, обладающий структурными характеристиками, схожими с таковыми мембран транспортных везикул (COPII), а также их вспомогательных партнеров (HOPS/CORVET) и ядерной поры (NPC). Дрожжевой SEA-комплекс динамически взаимодействует с вакуолями. Данные о функции SEA-комплекса очень малочисленны. В представленном миниобзоре обсуждается возможная функция SEA-комплекса, основываясь на результатах генетических и функциональных исследований, проведенных на дрожжах и других эукариотах. Ключевые слова: дрожжи Saccharomyces cerevisiae, SEA-комплекс, вакуоли. Наявність різноманітних внутрішньоклітинних мембранних органел, динамічно пов’язаних за посередництвом селективного транспорту, є відмінною особливістю еукаріотичної клитини. Багато білків, необхідних для утворення та існування цих органел, мають подібну еволюційну історію. Недавно ми відкрили новий консервативний білковый комплекс – SEA-комплекс, якому притаманні структурні характеристики, схожі з такими мембран транспортных везикул (COPII) та їхніх допоміжних партнерів (HOPS/ CORVET) і ядерної пори (NPC). Дріжджовий SEA-комплекс динамічно взаємодіє з вакуолями. Дані щодо функції SEA-комплексу є доволі малочисельними. В представленому мініогляді обговорюється можлива функція SEA-комплексу з урахуванням результатів генетичних і функціональних досліджень, проведених на дріжджах та інших еукаріотах. Ключові слова: дріжджі Saccharomyces cerevisiae, SEA-комплекс, вакуолі. The presence of distinctive internal membrane compartments, dynamically connected via selective transport pathways, is a hallmark of eukaryotic cells. Many of the proteins required for formation and maintenance of these compartments share an evolutionary history. We have recently identified a new conserved protein complex – the SEA complex – that possesses proteins with structural characteristics similar to the membrane coating complexes such as the nuclear pore complex (NPC), the COPII vesicle coating complex and HOPS/CORVET tethering complexes. The SEA complex in yeast is dynamically associated to the vacuole. The data on the function of the SEA complex remain extremely limited. Here we will discuss a possible role of the SEA complex based on the data from genetic assays and a number of functional studies in both yeast and other eukaryotes. Keywords: Saccharomyces cerevisiae, the SEA complex, vacuoles. en Інститут молекулярної біології і генетики НАН України Вiopolymers and Cell Minireviews The SEA complex – the beginning SEA-комплекс – початок SEA-комплекс – начало Article published earlier |
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Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| collection |
DSpace DC |
| title |
The SEA complex – the beginning |
| spellingShingle |
The SEA complex – the beginning Algret R. Dokudovskaya, S.S. Minireviews |
| title_short |
The SEA complex – the beginning |
| title_full |
The SEA complex – the beginning |
| title_fullStr |
The SEA complex – the beginning |
| title_full_unstemmed |
The SEA complex – the beginning |
| title_sort |
sea complex – the beginning |
| author |
Algret R. Dokudovskaya, S.S. |
| author_facet |
Algret R. Dokudovskaya, S.S. |
| topic |
Minireviews |
| topic_facet |
Minireviews |
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2012 |
| language |
English |
| container_title |
Вiopolymers and Cell |
| publisher |
Інститут молекулярної біології і генетики НАН України |
| format |
Article |
| title_alt |
SEA-комплекс – початок SEA-комплекс – начало |
| description |
Наличие разнообразных внутриклеточных мембранных органелл, динамически связанных посредством селективного транспорта, является отличительной особенностью эукариотической клетки. Множество белков, необходимых для образования и существования этих органелл, имеют сходную эволюционную историю. Недавно мы открыли новый консервативный белковый комплекс – SEA-комплекс, обладающий структурными характеристиками, схожими с таковыми мембран транспортных везикул (COPII), а также их вспомогательных партнеров (HOPS/CORVET) и ядерной поры (NPC). Дрожжевой SEA-комплекс динамически взаимодействует с вакуолями. Данные о функции SEA-комплекса очень малочисленны. В представленном миниобзоре обсуждается возможная функция SEA-комплекса, основываясь на результатах генетических и функциональных исследований, проведенных на дрожжах и других эукариотах.
Ключевые слова: дрожжи Saccharomyces cerevisiae, SEA-комплекс, вакуоли.
Наявність різноманітних внутрішньоклітинних мембранних органел, динамічно пов’язаних за посередництвом селективного транспорту, є відмінною особливістю еукаріотичної клитини. Багато білків, необхідних для утворення та існування цих органел, мають подібну еволюційну історію. Недавно ми відкрили новий консервативний білковый комплекс – SEA-комплекс, якому притаманні структурні характеристики, схожі з такими мембран транспортных везикул (COPII) та їхніх допоміжних партнерів (HOPS/ CORVET) і ядерної пори (NPC). Дріжджовий SEA-комплекс динамічно взаємодіє з вакуолями. Дані щодо функції SEA-комплексу є доволі малочисельними. В представленому мініогляді обговорюється можлива функція SEA-комплексу з урахуванням результатів генетичних і функціональних досліджень, проведених на дріжджах та інших еукаріотах.
Ключові слова: дріжджі Saccharomyces cerevisiae, SEA-комплекс, вакуолі.
The presence of distinctive internal membrane compartments, dynamically connected via selective transport pathways, is a hallmark of eukaryotic cells. Many of the proteins required for formation and maintenance of these compartments share an evolutionary history. We have recently identified a new conserved protein complex – the SEA complex – that possesses proteins with structural characteristics similar to the membrane coating complexes such as the nuclear pore complex (NPC), the COPII vesicle coating complex and HOPS/CORVET tethering complexes. The SEA complex in yeast is dynamically associated to the vacuole. The data on the function of the SEA complex remain extremely limited. Here we will discuss a possible role of the SEA complex based on the data from genetic assays and a number of functional studies in both yeast and other eukaryotes.
Keywords: Saccharomyces cerevisiae, the SEA complex, vacuoles.
|
| issn |
0233-7657 |
| url |
https://nasplib.isofts.kiev.ua/handle/123456789/156925 |
| citation_txt |
The SEA complex – the beginning / R.Algret, S.S. Dokudovskaya // Вiopolymers and Cell. — 2012. — Т. 28, № 4. — С. 281–284. — Бібліогр.: 20 назв. — англ. |
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2025-11-27T04:34:21Z |
| last_indexed |
2025-11-27T04:34:21Z |
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| fulltext |
281
MINIREVIEWS
UDC 577.22
The SEA complex – the beginning
R. Algret, S. S. Dokudovskaya
CNRS UMR 8126, UniversitJ Paris-Sud 11, Institut Gustave Roussy
114, rue Edouard Vaillant, Villejuif, France, 94805
s.dokud@gmail.com
The presence of distinctive internal membrane compartments, dynamically connected via selective transport
pathways, is a hallmark of eukaryotic cells. Many of the proteins required for formation and maintenance of these
compartments share an evolutionary history. We have recently identified a new conserved protein complex – the
SEA complex – that possesses proteins with structural characteristics similar to the membrane coating comp-
lexes such as the nuclear pore complex (NPC), the COPII vesicle coating complex and HOPS/CORVET tethe-
ring complexes. The SEA complex in yeast is dynamically associated to the vacuole. The data on the function of the
SEA complex remain extremely limited. Here we will discuss a possible role of the SEA complex based on the
data from genetic assays and a number of functional studies in both yeast and other eukaryotes.
Keywords: Saccharomyces cerevisiae, the SEA complex, vacuoles.
What is the SEA complex? The SEA complex is a ~1 MDa
protein complex that was discovered in yeast Saccharo-
my ces cerevisiae during immunopurification of genomi-
cally tagged version of one of the components of the NPC,
the nucleoporin Seh1 [1]. As a bone fide nucleoporin,
Seh1 co-purifies with the Nup84 subcomplex, a key com-
ponent of the NPC’s membrane-coating scaffold. How-
ever, Seh1 also co-purifies with Npr2, Npr3, Sec13 and
four high-molecular-weight proteins (Yjr138p (Iml1),
Yol138p (Rtc1), Ydr128p (Mtc5), and Ybl104p). To ref-
lect their association with Seh1, these proteins were gi-
ven a common name, Sea (for Seh1-associated), and were
renamed Sea1 through Sea4, respectively. Tagged ver-
sions of each of Sea1–Sea4 copurified with each other,
and with Seh1, Sec13, Npr2, and Npr3. Sec13 is also a
member of the NPC’s Nup84 subcomplex. In addition,
Sec13 interacts with Sec31 in ER-trafficking COPII
vesicles; however, other NPC proteins or members of
COPII vesicles were not found to be associated with the
Sea proteins, and the Sea proteins did not localize to the
NPC or ER, confirming that this group of proteins forms
a novel and distinct complex, the SEA complex, entire-
ly separate from the NPC or COPII.
How conserved is the SEA complex? The full SEA
complex is specific to animals and fungi [1]. There is
no evidence for any SEA complex gene in plants (with
the exception of Seh1 and Sec13, which certainly fulfill
other functions in this lineage). In other eukaryotic su-
pergroups the SEA complex members are not always re-
tained. The evolutionary profile of the SEA complex
suggests that it might be dispensable in many biolo-
gical contexts, having a specialized life-style specific
role rather than a function central to eukaryotic fitness.
Where is the SEA complex localized? The expres-
sion level of the SEA complexes members is very low
both in yeast and in human cells, which make the task
of their localization challenging. Nevertheless the com-
bination of subcellular fractionation and fluorescent
microscopy detected yeast SEA complex as dynamical-
ly associated to the vacuole membrane [1]. The proteo-
mic study of human placenta lysosomes also found ho-
mologues of Sea1, Sea2, Sea4, Seh1, and Sec13 to be as-
sociated to the lysosomal membrane [2]. However, be-
cause of the low level of expression of the SEA comp-
lex components it is possible that they can be found el-
sewhere in the cell.
What is the structural specificity of the SEA comp-
lex members? Sea proteins contain structural elements
ISSN 0233–7657. Biopolymers and Cell. 2012. Vol. 28. N 4. P. 281–284
Ó Institute of Molecular Biology and Genetics, NAS of Ukraine, 2012
present in intracellular structural trafficking complexes
[1]. For example, the Sea2-Sea4 proteins are predicted
to possess a b-propeller/a-solenoid architecture charac-
teristic of proteins that form coats around membranes
and participate in membrane tethering. Notably, SEA
complex contains five proteins with b-propellers, a do-
main common in coating assemblies. Among those pro-
teins with b-propellers are Seh1 and Sec13 – two evolu-
tionary conserved paraloges that are known members
of other coating assemblies – NPC (both proteins) and
COPII (Sec13 only). Seh1 forms a dimer with Sea4,
which besides b-propeller and a-solenoid, contains a
C-terminal RING domain. The structural organization
of the Sea4 is identical to a number of proteins in HOPS
and CORVET complexes, which have been implicated
in tethering membranes together prior to their fusion.
Similar to several proteins of HOPS/CORVET Sea2–
Sea4 have a C-terminal RING domain. The high fre-
quency of RING domains in the SEA complex suggests
that the complex may act as an E3 ubiquitin ligase.
What did we learn about SEA complex function from
yeast studies? Not too much so far. The majority of the
data concerns Npr2 and Npr3. These two proteins in
yeast act as upstream regulators of TORC1 kinase in
response to nitrogen starvation [3]. Accordingly, the
process of autophagy, which is induced in the response
to nitrogen starvation, is impaired in the absence of
Npr2 and to some extent of Npr3 [1, 4]. Interestingly,
Npr2, Npr3 and Sea1 also required for a specific varia-
tion of autophagy, which can be induced in the absence
of nitrogen starvation, but simply upon the change from
rich to a minimal medium [5].
Otherwise SEA complex deletion strains exhibited
relatively robust growth under a broad range of tests [1]
(http://www.yeastgenome.org/). This presumes that the
SEA complex functions alongside other related comp-
lexes and may be redundant under numerous growth
conditions. However, complete redundancy is unlike-
ly given evolutionary conservation of SEA complex
subunits, especially in the animals and fungi. Recent
papers on yeast synthetic genetic interactions [6] and
chemical genetic profiles [7] shed a bit of a light on a
possible role of the SEA complex. Analysis of these
data suggests that SEA complex members are impli-
cated in multiple genetic interactions with genes res-
ponsible for cell wall biogenesis and integrity, amino
acid biogenesis and sorting, membrane trafficking,
ubiquitination and autophagy.
One of the strongest genetic interactions that invol-
ve SEA complex members is the cooperation with the
genes responsible for cell wall biogenesis and integri-
ty. Thus, all five SEA complex genes appeared in Cos-
tanzo et al. [6] survey exhibit genetic interaction with
MAP kinase Bck1; four SEA complex genes involved
in genetic interaction with another MAP kinase – Slt2.
In addition, Sea4 is synthetically lethal with Las21 – an
integral plasma membrane protein involved in the syn-
thesis of the glycosylphosphatidylinositol (GPI) core
structure [8]. Similar to SEA complex genes Las21 is
involved in negative genetic interactions with Pkc1 and
Slt2 [6] and synthetically lethal with Bck1 [8].
A gene cohort involved in amino acid biosynthesis
and sorting exhibits a large number of strong genetic in-
teractions with SEA complex subunits. Notably, HOPS/
CORVET belongs to this same interaction cluster [6],
further underscoring the similarity between these comp-
lexes and the SEA complex. One module in the cluster
is responsible for sorting of a general amino acid per-
mease Gap1. Gap1 is a general amino acid permease
that can transport all amino acids. GAP1 is transcriptio-
nally regulated by the available nitrogen source via nit-
rogen catabolite repression (NCR). Interestingly, both
Npr2 and Npr3 are probably involved in the NCR cont-
rol [9]. Gap1 sorting is mediated by number of proteins
and complexes, including EGO complex, Lst proteins
and Rsp5-Bul1-Bul2 trimer, which ubiquitinate Gap1
itself. All of these genes display genetic interactions
with the SEA complex members. In addition chemical
genomic survey reports that Sea2, Sea4 and Sec13 show
similar homozygous co-fitness with a number of genes
involved in Gap1 sorting [7].
The most striking examples of SEA components ge-
netic interaction is connection with genes involved in the
biosynthesis of homoserine with almost entire set of the
genes responsible for this pathway exhibiting very strong
genetic interactions with 4 or 5 SEA complex members
[6]. The majority of amino acids biosynthesis pathway
genes, including those, involved in the genetic interac-
tions with SEA complex genes are regulated by Gcn4
transcriptional activator [10]. Strikingly, Sea4 has mul-
tiple Gcn4 binding sites in its promoter [11], and there-
fore can be implicated in the control of amino acid biosyn-
282
ALGRET R., DOKUDOVSKAYA S. S.
thesis. Interestingly, a chemical genomic survey identi-
fied a small group of genes, required for resistance to di-
verse perturbations [7]. These genes referred to as multi-
drug resistance (MDR). Genes that involved in aromatic
amino acid biosynthesis (and synthetic genetic interac-
tions with SEA components), GCN4 and NPR2 together
with NPR3 are all belong to the MDR group. By the way,
NPR2 and NPR3 exhibit absolutely identical co-fitness
of respective homozygous deletion strains in chemical
genomic survey, which is a strong indication for these
two proteins share similar biological process and mo-
lecular function [7]. All the observations described
here suggest that the SEA complex plays a role in the
regu- lation of amino acid biosynthesis and autophagy.
What do we know about SEA complex components in
high eukaryotes? The fact that all SEA complex mem-
bers were retained in higher eukaryotes underlines func-
tional importance of this assembly. Nevertheless, infor-
mation about SEA complex components in higher euka-
ryotes is even more limited than in yeast. So far no pa-
pers were published on Sea1, Sea2, Sea3 homologues.
Sea4 homologue in Drosophila (missing oocyte, mio)
is localized to the nucleus and required for the mainte-
nance of the meiotic cycle and oocyte identity [12]. Im-
portantly, Mio forms a complex with Seh1. Both pro-
teins are dispensable for somatic development, but re-
quired for development of the mature egg. In addition
Seh1 is required for Mio protein stability [13]. Human
Seh1 also functions in chromosome alignment and se-
gregation by regulating the centromeric localization of
Aurora B and other chromosome passenger complex
proteins [14]. Although Sea1-Sea4 and Npr2, Npr3
seems not to be present in plants, Seh1 in Arabidopsis
is found in multiple locations, including nucleus, Golgi
and prevacuolar compartment. AtSeh1 is suggested to
play a role in membrane association of dynamin-rela-
ted protein 2A, which is in turn required for protein traf-
ficking from trans-Golgi network to the central vacuole
[15]. Npr2 homologue in human – Nprl2 – has been cha-
racterized as a novel tumor suppressor [16]. Low ex-
pression of Nprl2 in different types of lung cancers and
other tumors was correlated with resistance to cisplatin,
one of the mainstays of chemotherapy for lung cancer
[17]. Remarkably, the first information about cisplatin
resistance of Npr2 deletion strains came from the stu-
dies in yeast [18]. Nprl2 interacts with Pdk1 kinase, a
key regulator of cell proliferation and survival [19].
Interestingly, Pdk1, which plays a role in cellular trans-
formation and tumor growth, is one of the well-defined
upstream regulators of TORC1 pathway in mammalian
cells. In addition Nprl2 forms a complex with Npr3
homologue Nprl3 [3], which suggests that Nprl2/Nprl3
might also signal to TORC1, similar to their yeast coun-
terparts. Finally a recent study has demonstrated that
Nprl3 (C16orf35) is a nucleocytoplasmic protein that
interacts with transcriptional factor p73, a member of
p53 family proteins involved in tumor suppression and
embryonic development [20].
What are the future directions in the SEA complex
study? The study of the SEA complex is in its primary
steps and all directions are open and have to be explo-
red. The importance of the SEA complex is underlined
by the fact that all of its components have been retained
in animals and fungi. The integrative approaches which
can combine data on structure, function, regulation and
coming from different model organisms should be the
most informative. The results of these studies might be
of a broad interest given that the Nprl2 in human has
been characterized as a novel tumor suppressor [16]
and the Nprl3 interacts with p73 [20] – a member of
p53 family of transcription factors involved in tumor
suppression.
Acknowledgements. We are grateful to the support
from Fondation de France, Fondation pour la Recher-
che Medicale and Fondation Gustave Roussy.
Ð. Àëãðå, Ñ. Ñ. Äî êó äî âñüêà
SEA-êîì ïëåêñ – ïî ÷à òîê
Ðå çþ ìå
Íà ÿâí³ñòü ð³çíî ìàí³òíèõ âíóòð³øíüîêë³òèí íèõ ìåì áðàí íèõ îðãà-
íåë, äè íàì³÷íî ïî â’ÿ çà íèõ çà ïî ñå ðåä íèö òâîì ñå ëåê òèâ íî ãî òðàíñ-
ïîðòó, º â³äì³ííîþ îñîá ëèâ³ñòþ åó êàð³îò è÷ íî¿ êëè òè íè. Áà ãà òî
á³ëê³â, íå îáõ³äíèõ äëÿ óòâî ðåí íÿ òà ³ñíó âàí íÿ öèõ îðãà íåë, ìà þòü
ïîä³áíó åâî ëþö³éíó ³ñòîð³þ. Íå äàâ íî ìè â³äêðè ëè íî âèé êîí ñåð âà -
òèâ íèé á³ëêî âûé êîì ïëåêñ – SEA-êîì ïëåêñ, ÿêî ìó ïðè òà ìàíí³
ñòðóê òóðí³ õà ðàê òå ðèñ òè êè, ñõîæ³ ç òà êè ìè ìåì áðàí òðàíñ -
ïîð òíûõ âå çè êóë (COPII) òà ¿õí³õ äî ïîì³æíèõ ïàð òíåð³â (HOPS/
CORVET) ³ ÿäåð íî¿ ïîðè (NPC). Äð³æäæî âèé SEA-êîì ïëåêñ äè -
íàì³÷íî âçàºìî䳺 ç âà êó î ëÿ ìè. Äàí³ ùîäî ôóíêö³¿ SEA-êîì ïëåê ñó
º äî âîë³ ìà ëî ÷è ñåëü íè ìè.  ïðåä ñòàâ ëå íî ìó ì³í³îãëÿä³ îá ãî âî ðþ-
ºòüñÿ ìîæ ëè âà ôóíêö³ÿ SEA-êîì ïëåê ñó ç óðà õó âàí íÿì ðå çóëü òà-
ò³â ãå íå òè÷ íèõ ³ ôóíêö³îíàëü íèõ äîñë³äæåíü, ïðî âå äå íèõ íà äð³æä-
æàõ òà ³íøèõ åó êàð³îòàõ.
Êëþ ÷îâ³ ñëî âà: äð³æäæ³ Saccharomyces cerevisiae, SEA-êîìï-
ëåêñ, âà êó îë³.
283
THE SEA COMPLEX – THE BEGINNING
ALGRET R., DOKUDOVSKAYA S. S.
Ð. Àëãðå, Ñ. Ñ. Äî êó äîâ ñêàÿ
SEA-êîì ïëåêñ – íà ÷à ëî
Ðå çþ ìå
Íà ëè ÷èå ðàç íî îá ðàç íûõ âíóò ðèê ëå òî÷ íûõ ìåì áðàí íûõ îðãà íåëë,
äè íà ìè ÷åñ êè ñâÿ çàí íûõ ïî ñðå äñòâîì ñå ëåê òèâ íî ãî òðàíñ ïîð òà,
ÿâ ëÿ åò ñÿ îò ëè ÷è òåëü íîé îñî áåí íîñ òüþ ýó êà ðè î òè ÷åñ êîé êëåò -
êè. Ìíî æåñ òâî áåë êîâ, íå îá õî äè ìûõ äëÿ îá ðà çî âà íèÿ è ñó ùåñò-
âî âà íèÿ ýòèõ îðãà íåëë, èìå þò ñõîä íóþ ýâî ëþ öè îí íóþ èñ òî ðèþ.
Íå äàâ íî ìû îò êðû ëè íî âûé êîí ñåð âà òèâ íûé áåë êî âûé êîì ïëåêñ –
SEA-êîì ïëåêñ, îá ëà äà þ ùèé ñòðóê òóð íû ìè õà ðàê òå ðèñ òè êà ìè,
ñõî æè ìè ñ òà êîâû ìè ìåì áðàí òðàíñ ïîð òíûõ âå çè êóë (COPII), à
òàê æå èõ âñïî ìî ãà òåëü íûõ ïàð òíå ðîâ (HOPS/CORVET) è ÿäåð -
íîé ïîðû (NPC). Äðîæ æå âîé SEA-êîì ïëåêñ äè íà ìè ÷åñ êè âçà è ìî -
äå éñòâó åò ñ âà êó î ëÿ ìè. Äàí íûå î ôóíê öèè SEA-êîì ïëåê ñà î÷åíü
ìà ëî ÷èñ ëåí íû.  ïðåä ñòàâ ëåí íîì ìè íè îá çî ðå îá ñóæ äà åò ñÿ âîç -
ìîæíàÿ ôóíê öèÿ SEA-êîì ïëåê ñà, îñíî âû âà ÿñü íà ðå çóëü òà òàõ ãå-
íåòè ÷åñ êèõ è ôóíê öè î íàëü íûõ èñ ñëå äî âà íèé, ïðî âå äåí íûõ íà äðîæ-
æàõ è äðó ãèõ ýó êà ðè î òàõ.
Êëþ ÷å âûå ñëî âà: äðîæ æè Saccharomyces cerevisiae, SEA-êîìï-
ëåêñ, âà êó î ëè.
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