The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1

Kloks, Cathelijne P. A. M.; Spronk, Chris A. E. M.; Lasonder, Edwin; Hoffmann, Adrian; Vuister, Geerten W.; Grzesiek, Stephan; Hilbers, Cornelis W.

doi:10.1006/jmbi.2001.5334

Cited by 123 publications

(144 citation statements)

References 44 publications

Supporting

Mentioning

136

Contrasting

Order By: Relevance

“…Upon such interaction, according to an entropy transfer model, unfolding of RNA secondary structure may be accompanied by folding of natively unfolded regions of RNA chaperones (Tompa & Csermely, 2004). Several wellstudied RNA chaperones such as YB-1, the major protein of messenger RNP complexes, and E. coli regulatory protein StpA have a bipartite structure composed of two domains, one of which is stably folded, exhibiting RNAbinding and/or protein oligomerization activity, whereas another is natively unfolded, containing sites of RNA chaperone activity (Matsumoto & Wolffe, 1998;Kloks et al, 2002;Mayer et al, 2007;Rajkowitsch et al, 2007). The PSLV TGBp1 N-terminal extension region is organized in a similar way, with RNA binding and protein oligomerization functions associated with the structured ID and another RNA-binding activity associated with the natively unfolded NTD.…”

Section: Discussionmentioning

confidence: 99%

Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1

Makarov

Rybakova

Ефимов

et al. 2009

Journal of General Virology

View full text Add to dashboard Cite

Three 'triple gene block' proteins known as TGBp1, TGBp2 and TGBp3 are required for cell-tocell movement of plant viruses belonging to a number of genera including Hordeivirus. Hordeiviral TGBp1 interacts with viral genomic RNAs to form ribonucleoprotein (RNP) complexes competent for translocation between cells through plasmodesmata and over long distances via the phloem. Binding of hordeivirus TGBp1 to RNA involves two protein regions, the C-terminal NTPase/ helicase domain and the N-terminal extension region. This study demonstrated that the extension region of hordeivirus TGBp1 consists of two structurally and functionally distinct domains called the N-terminal domain (NTD) and the internal domain (ID). In agreement with secondary structure predictions, analysis of circular dichroism spectra of the isolated NTD and ID demonstrated that the NTD represents a natively unfolded protein domain, whereas the ID has a pronounced secondary structure. Both the NTD and ID were able to bind ssRNA non-specifically. However, whilst the NTD interacted with ssRNA non-cooperatively, the ID bound ssRNA in a cooperative manner. Additionally, both domains bound dsRNA. The NTD and ID formed low-molecular-mass oligomers, whereas the ID also gave rise to high-molecular-mass complexes. The isolated ID was able to interact with both the NTD and the C-terminal NTPase/helicase domain in solution. These data demonstrate that the hordeivirus TGBp1 has three RNA-binding domains and that interaction between these structural units can provide a basis for remodelling of viral RNP complexes at different steps of cell-to-cell and long-distance transport of virus infection. INTRODUCTIONTransport of plant viruses from cell to cell occurs through plasmodesmata and requires virus-encoded movement proteins (Boevink & Oparka, 2005;Lucas, 2006;Epel, 2009). In the genus Hordeivirus, viral movement proteins are represented by three proteins encoded by a 'triple gene block' (TGB) and referred to as TGBp1, TGBp2 and TGBp3 (Solovyev et al., 1996). The TGB is a conserved module of overlapping genes found in a number of virus groups (Morozov & Solovyev, 2003). Hordeivirus TGBp1 binds viral genomic RNA forming a cell-to-cell transportcompetent complex (Brakke et al., 1988;Kalinina et al., 2001;Lim et al., 2008;Jackson et al., 2009). TGBp2 and TGBp3 are small membrane proteins necessary for intracellular transport of complexes containing TGBp1 and viral RNA to plasmodesmata (Morozov & Solovyev, 2003;Zamyatnin et al., 2004; Haupt et al., 2005;Jackson et al., 2009 Lim et al., 2008;Jackson et al., 2009). Such TGBp1-RNA complexes are considered to be a form of viral genome capable of cell-to-cell and long-distance transport in plants (Morozov & Solovyev, 2003;Lim et al., 2008). In potex-like TGBs, the whole TGBp1 sequence is represented by the NTPase/helicase domain (HELD) with seven conserved motifs of the superfamily 1 NTPases/helicases (Gorbalenya et al., 1989), whereas the hordei-like TGBp1 has an additional N-terminal 'extension region' (Morozov & Solovyev, ...

show abstract

Section: Discussionmentioning

confidence: 99%

Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1

Makarov

Rybakova

Ефимов

et al. 2009

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…Residues within these motifs facilitate RNA binding by making direct contacts with the nucleic acid, which is required for cytoplasmic localization (Kloks et al, 2002;Bader et al, 2003). Mutation of single residues in these domains abrogates RNA binding and induces nuclear translocation (Bouvet et al, 1995;Bader et al, 2003).…”

mentioning

confidence: 99%

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Bader

Vogt

2007

Oncogene

View full text Add to dashboard Cite

The Y box-binding protein 1 (YB-1) is a DNA/RNAbinding protein that regulates mRNA transcription and translation. It is a major component of free messenger ribonucleoprotein particles and, at higher concentrations, blocks protein synthesis. In chicken embryo fibroblasts, overexpression of YB-1 confers a specific resistance to oncogenic cellular transformation by phosphoinositide 3-kinase (PI3K) or Akt/PKB. Recent studies have identified YB-1 as a direct substrate of Akt. The functional significance of Akt-mediated phosphorylation remains largely unknown. We generated YB-1 mutants in the Akt phosphorylation consensus sequence to explore the effect of phosphorylated YB-1 in PI3K-induced transformation. In contrast to wild-type YB-1, the phosphomimetic S99E mutant no longer interferes with cellular transformation. This mutant has reduced affinity for the cap of mRNAs and fails to inhibit cap-dependent translation. The data suggest that phosphorylation by Akt disables the inhibitory activity of YB-1 and thereby enhances the translation of transcripts that are necessary for oncogenesis. Overexpression of wild-type YB-1 overrides inactivation by Akt and maintains inhibition of protein synthesis and resistance to transformation.

show abstract

“…Among bacterial Csps and YB-1, the ~70 residues that comprise the CSD represent the only region that exhibits a high level of sequence conservation. Studies on the CSD of YB-1 revealed a β-barrel spatial structure bearing similarity to bacterial Csps with a similar arrangement of RNA binding motifs (5,10,13). The C-terminal auxiliary domain was proposed to have a nonspecific affinity for RNA and DNA which may result from its interaction with negatively charged phosphate groups of nucleic acids (14).…”

Section: Structure Of Cold Shock Domain Proteinsmentioning

confidence: 99%

The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1

Cited by 123 publications

References 44 publications

Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1

Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins

Contact Info

Product

Resources

About