Role of Proteins Interacting with the eRF1 and eRF3 Release Factors in the Regulation of Translation and Prionization

Standard

Role of Proteins Interacting with the eRF1 and eRF3 Release Factors in the Regulation of Translation and Prionization. / Zhouravleva, G. A.; Bondarev, S. A.; Zemlyanko, O. M.; Moskalenko, S. E.

In: Molecular Biology, Vol. 56, No. 2, 01.04.2022, p. 147-165.

Research output: Contribution to journal › Review article › peer-review

BibTeX

@article{fd69b5476be641f5bb776a0ae7c25e13,

title = "Role of Proteins Interacting with the eRF1 and eRF3 Release Factors in the Regulation of Translation and Prionization",

abstract = "Abstract: The review discusses the role that proteins interacting with the translation termination factors eRF1 and eRF3 play in the control of protein synthesis and prionization. These proteins interact not only with each other, but also with many other proteins involved in controlling the efficiency of translation termination, and associate translation termination with other cell processes. The termination of translation is directly related not only to translation re-initiation and ribosome recycling, but also to mRNA stability and protein quality control. This connection is ensured by the interaction of eRF1 and eRF3 with proteins participating in various cell metabolic processes, such as mRNA transport from the nucleus into the cytoplasm (Dbp5/DDX19 and Gle1), ribosome recycling (Rli1/ABCE1), mRNA degradation (Upf proteins), and translation initiation (Pab1/PABP). In addition to genetic control, there is epigenetic control of translation termination. This mechanism is associated with prion polymerization of the Sup35 protein to form the [PSI+] prion. The maintenance of the [PSI+] prion, like other yeast prions, requires the operation of a system of molecular chaperones and protein sorting factors. The review considers in detail the interaction of the translation termination factors with proteins involved in various cellular processes.",

keywords = "eRF1, eRF3, PABP, prion, protein quality control, SUP35, SUP45, translation termination, Upf, [PSI], [PSI+]",

author = "Zhouravleva, {G. A.} and Bondarev, {S. A.} and Zemlyanko, {O. M.} and Moskalenko, {S. E.}",

note = "Publisher Copyright: {\textcopyright} 2022, Pleiades Publishing, Inc.",

year = "2022",

month = apr,

day = "1",

doi = "10.1134/s0026893322010101",

language = "English",

volume = "56",

pages = "147--165",

journal = "Molecular Biology",

issn = "0026-8933",

publisher = "Pleiades Publishing",

number = "2",

}

RIS

TY - JOUR

T1 - Role of Proteins Interacting with the eRF1 and eRF3 Release Factors in the Regulation of Translation and Prionization

AU - Zhouravleva, G. A.

AU - Bondarev, S. A.

AU - Zemlyanko, O. M.

AU - Moskalenko, S. E.

PY - 2022/4/1

Y1 - 2022/4/1

N2 - Abstract: The review discusses the role that proteins interacting with the translation termination factors eRF1 and eRF3 play in the control of protein synthesis and prionization. These proteins interact not only with each other, but also with many other proteins involved in controlling the efficiency of translation termination, and associate translation termination with other cell processes. The termination of translation is directly related not only to translation re-initiation and ribosome recycling, but also to mRNA stability and protein quality control. This connection is ensured by the interaction of eRF1 and eRF3 with proteins participating in various cell metabolic processes, such as mRNA transport from the nucleus into the cytoplasm (Dbp5/DDX19 and Gle1), ribosome recycling (Rli1/ABCE1), mRNA degradation (Upf proteins), and translation initiation (Pab1/PABP). In addition to genetic control, there is epigenetic control of translation termination. This mechanism is associated with prion polymerization of the Sup35 protein to form the [PSI+] prion. The maintenance of the [PSI+] prion, like other yeast prions, requires the operation of a system of molecular chaperones and protein sorting factors. The review considers in detail the interaction of the translation termination factors with proteins involved in various cellular processes.

AB - Abstract: The review discusses the role that proteins interacting with the translation termination factors eRF1 and eRF3 play in the control of protein synthesis and prionization. These proteins interact not only with each other, but also with many other proteins involved in controlling the efficiency of translation termination, and associate translation termination with other cell processes. The termination of translation is directly related not only to translation re-initiation and ribosome recycling, but also to mRNA stability and protein quality control. This connection is ensured by the interaction of eRF1 and eRF3 with proteins participating in various cell metabolic processes, such as mRNA transport from the nucleus into the cytoplasm (Dbp5/DDX19 and Gle1), ribosome recycling (Rli1/ABCE1), mRNA degradation (Upf proteins), and translation initiation (Pab1/PABP). In addition to genetic control, there is epigenetic control of translation termination. This mechanism is associated with prion polymerization of the Sup35 protein to form the [PSI+] prion. The maintenance of the [PSI+] prion, like other yeast prions, requires the operation of a system of molecular chaperones and protein sorting factors. The review considers in detail the interaction of the translation termination factors with proteins involved in various cellular processes.

KW - eRF1

KW - eRF3

KW - PABP

KW - prion

KW - protein quality control

KW - SUP35

KW - SUP45

KW - translation termination

KW - Upf

KW - [PSI]

KW - [PSI+]

UR - http://www.scopus.com/inward/record.url?scp=85128293643&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/c3991df3-00a4-3b38-bc21-79fb0795d903/

U2 - 10.1134/s0026893322010101

DO - 10.1134/s0026893322010101

M3 - Review article

AN - SCOPUS:85128293643

VL - 56

SP - 147

EP - 165

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 100122430