Functional and structural characterization of novel type of linker connecting capsid and nucleocapsid protein domains in murine leukemia virus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F16%3A43901681" target="_blank" >RIV/60461373:22330/16:43901681 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/16:00466261

Result on the web

<a href="http://dx.doi.org/10.1074/jbc.M116.746461" target="_blank" >http://dx.doi.org/10.1074/jbc.M116.746461</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M116.746461" target="_blank" >10.1074/jbc.M116.746461</a>

Result language

angličtina

Original language name

Functional and structural characterization of novel type of linker connecting capsid and nucleocapsid protein domains in murine leukemia virus

Original language description

The assembly of immature retroviral particles is initiated in the cytoplasm by the binding of the structural polyprotein precursor Gag with viral genomic RNA. The protein interactions necessary for assembly are mediated predominantly by the capsid (CA) and nucleocapsid (NC) domains, which have conserved structures. In contrast, the structural arrangement of the CA-NC connecting region differs between retroviral species. In HIV-1 and Rous sarcoma virus, this region forms a rod-like structure that separates the CA and NC domains, whereas in Mason-Pfizer monkey virus, this region is densely packed, thus holding the CA and NC domains in close proximity. Interestingly, the sequence connecting the CA and NC domains in gammaretroviruses, such as murine leukemia virus (MLV), is unique. The sequence is called a charged assembly helix (CAH) due to a high number of positively and negatively charged residues. Although both computational and deletion analyses suggested that the MLV CAH forms a helical conformation, no structural or biochemical data supporting this hypothesis have been published. Using an in vitro assembly assay, alanine scanning mutagenesis, and biophysical techniques (circular dichroism, NMR, microcalorimetry, and electrophoretic mobility shift assay), we have characterized the structure and function of the MLV CAH. We provide experimental evidence that the MLV CAH belongs to a group of charged, E(R/K)-rich, single ?-helices. This is the first single ?-helix motif identified in viral proteins.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EI - Biotechnology and bionics

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2016

Confidentiality

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

Name of the periodical

JOURNAL OF BIOLOGICAL CHEMISTRY

ISSN

0021-9258

e-ISSN

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Volume of the periodical

291

Issue of the periodical within the volume

39

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

20630-20642

UT code for WoS article

000384574800027

EID of the result in the Scopus database

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