The extreme N-terminal domain of a hordeivirus TGB1 movement protein mediates its localization to the nucleolus and interaction with fibrillarin

Biochimie
M A SemashkoNatalia O Kalinina

Abstract

The hordeiviral movement protein encoded by the first gene of the triple gene block (TGBp1) of Poa semilatent virus (PSLV), interacts with viral genomic RNAs to form RNP particles which are considered to be a form of viral genome capable of cell-to-cell and long-distance transport in infected plants. The PSLV TGBp1 contains a C-terminal NTPase/helicase domain (HELD) and an N-terminal extension region consisting of two structurally and functionally distinct domains: an extreme N-terminal domain (NTD) and an internal domain (ID). This study demonstrates that transient expression of TGBp1 fused to GFP in Nicotiana benthamiana leaves results in faint but obvious fluorescence in the nucleolus in addition to cytosolic distribution. Mutagenesis of the basic amino acids inside the NTD clusters A (116)KSKRKKKNKK(125) and B (175)KKATKKESKKQTK(187) reveals that these clusters are indispensable for nuclear and nucleolar targeting of PSLV TGBp1 and may contain nuclear and nucleolar localization signals or their elements. The PSLV TGBp1 is able to bind to fibrillarin, the major nucleolar protein (AtFib2 from Arabidopsis thaliana) in vitro. This protein-protein interaction occurs between the glycine-arginine-rich (GAR) domain of fibrillarin a...Continue Reading

References

Dec 1, 1990·Virology·I T Petty, A O Jackson
May 1, 1996·The Journal of General Virology·C BleykastenG Jonard
Oct 20, 2000·The Journal of Biological Chemistry·M R HodelA E Hodel
May 29, 2003·The Journal of General Virology·Sergey Yu Morozov, Andrey G Solovyev
Dec 21, 2004·The Plant Cell·Sophie HauptLesley Torrance
Feb 19, 2005·Current Opinion in Structural Biology·Anthony L Fink
Aug 2, 2005·Trends in Biochemical Sciences·Peter TompaLászló Buday
Jan 17, 2007·Nature Reviews. Microbiology·Julian A Hiscox
Apr 6, 2007·The EMBO Journal·Sang Hyon KimMichael Taliansky
Mar 21, 2008·Journal of Virology·Hyoun-Sub LimAndrew O Jackson
Feb 21, 2009·EMBO Reports·Edward Emmott, Julian A Hiscox
Mar 11, 2009·Molecular Plant-microbe Interactions : MPMI·Lesley TorranceEugene I Savenkov
Apr 30, 2009·Annual Review of Phytopathology·Andrew O JacksonMi Yeon Lee
Feb 4, 2010·Molecular Plant-microbe Interactions : MPMI·Inmaculada GonzálezTomás Canto
Jul 20, 2010·Biochemistry. Biokhimii︠a︡·F V VityazevYu S Ovodov
Jul 29, 2010·The Biochemical Journal·Jens Tilsner, Karl J Oparka
Jun 11, 2011·The Open Virology Journal·Elena A ShemyakinaSergey Yu Morozov
Jul 26, 2011·Nucleic Acids Research·D V RakitinaN O Kalinina

❮ Previous
Next ❯

Citations

Aug 16, 2015·The Journal of General Virology·Valentin V MakarovNatalia O Kalinina
May 16, 2014·Chemical Reviews·Bin XueSonia Longhi
Aug 16, 2019·Molecular Plant-microbe Interactions : MPMI·Min XuRichard Kormelink
Feb 27, 2018·Frontiers in Plant Science·Natalia O KalininaMichael Taliansky
Feb 25, 2018·Current Opinion in Plant Biology·Svetlana Y Folimonova, Jens Tilsner
May 27, 2021·Molecular Biology Reports·Stefano Decle-CarrascoEnrique Castano

❮ Previous
Next ❯

Related Concepts

Related Feeds

Actin, Myosin & Cell Movement

Contractile forces generated by the actin-myosin cytoskeleton are critical for morphogenesis, but the cellular and molecular mechanisms of contraction have been elusive for many cell shape changes and movements. Here is the latest research on the roles of actin and myosin in cell movement.