N‐Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure

Makarov, Valentin V.; Taliansky, Michael; Добров, Е. Н.; Калинина, Н. В.

doi:10.1002/9781118135570.ch17

Cited by 2 publications

(9 citation statements)

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“…1b, solid line). Complexes with similar parameters and distribution were formed at 25 uC by the isolated ID and N63K, whereas the mean diameter of the NTD particles was *15 + 3 nm (Makarov et al, 2009(Makarov et al, , 2012. These complexes are formed spontaneously and are apparently unstable.…”

Section: Resultsmentioning

confidence: 87%

“…This effect can be explained by the phenomenon of 'cold denaturation' for proteins with loose tertiary structure -in the course of cooling, hydrophobic intramolecular interactions loosen, which leads to 'disintegration' of the tertiary structure of protein molecules with their subsequent aggregation due to intermolecular interactions (Privalov, 1990). Both N63K and ID, but not NTD, demonstrated similar properties (Makarov et al, 2010(Makarov et al, , 2012. Thus, ID is apparently the domain determining the ability of PSLV 63K protein for self-interaction.…”

Section: Resultsmentioning

confidence: 99%

“…The structure and formation mechanism of a non-virion transport form (RNP complex) by TGBp1 remain unclear. In our previous works (Makarov et al, 2010(Makarov et al, , 2012, we showed that the N-terminal extension region and the ID of PSLV TGBp1 can form in vitro multimeric filamentous structures. In this study, we demonstrate that the fulllength PSLV TGBp1 is also able to form similar highmolecular-mass complexes.…”

Section: Introductionmentioning

confidence: 86%

“…and HELD) obtained previously (Makarov et al, 2009(Makarov et al, , 2010(Makarov et al, , 2012. To assemble RNP particles, the TGBp1 has to be engaged in homologous protein-protein and protein-RNA interactions.…”

Section: V Makarov and Othersmentioning

confidence: 99%

“…Additionally, the hordeivirus TGBp1s have a long N-terminal extension region preceding the NTPase/ helicase domain that is variable in sequence and length with multiple RNA-binding sites (Donald et al, 1997;Kalinina et al, 2001;Morozov & Solovyev, 2003;Makarov et al, 2009). Combining several disorder prediction methods and experimental approaches, it was demonstrated that this region of the PSLV TGBp1 (referred to as N63K in our previous work; Kalinina et al, 2001) has large intrinsically disordered areas and consists of two domains -a completely intrinsically disordered extreme N-terminal domain (NTD) (aa and an internal domain (ID) (aa 200-290) with structure resembling a partially disordered molten globule (Makarov et al, 2009(Makarov et al, , 2012. Both domains demonstrate the ability for nonspecific RNA binding: NTD interacts with RNA noncooperatively and ID interacts cooperatively (Makarov et al, 2009); the whole N63K binds to RNA in a non-cooperative manner .…”

Section: Introductionmentioning

confidence: 96%

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In vitro properties of hordeivirus TGB1 protein forming ribonucleoprotein complexes

Makarov

Makarova

Makhotenko

et al. 2015

Journal of General Virology

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Hordeivirus movement protein encoded by the first gene of the triple gene block (TGB1 protein, TGBp1) interacts in vivo with viral genomic and subgenomic RNAs to form ribonucleoprotein (RNP) particles that are considered to be a form of viral genome (non-virion transport form) capable of cell-to-cell and long-distance transport in infected plants. The structures of these RNPs have not been elucidated. The poa semilatent virus (PSLV) TGBp1 contains a structured C-terminal NTPase/helicase domain and an N-terminal extension region consisting of two domains -a completely intrinsically disordered extreme N-terminal domain and an internal domain (ID) with structure resembling a partially disordered molten globule. Here, we characterized the structures assembled in vitro by the full-length PSLV TGBp1 alone or in the presence of viral RNA. The PSLV TGBp1 was capable of multimerization and self-assembly into extended high-molecular-mass complexes. These complexes disassembled to apparent monomers upon incubation with ATP. Upon incubation with viral RNA, the PSLV TGBp1 in vitro formed RNP structures that appeared as filamentous particles resembling virions of helical filamentous plant viruses in morphology and dimensions. By comparing the biophysical characteristics of PSLV TGBp1 and its domains in the presence and absence of RNA, we show that the ID plays the main structural role in the self-interactions and RNA interactions of TGBp1 leading to the assembly of virus-like RNP particles.

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Section: Resultsmentioning

confidence: 87%