Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25

Fujiwara, Takashi; Suzuki, Shunji; Kanno, Motoko; Sugiyama, H.; Takahashi, Hiroyuki; Tanaka, Junya

doi:10.1016/j.yexcr.2006.02.002

Cited by 19 publications

(11 citation statements)

References 26 publications

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“…The truncation of p42 removes K20 and K22, which form part of the nucleolar localisation signal (Squatrito et al , 2004). Such signals generally involve extended basic sequences (Fujiwara et al , 2006) and the structure of p48 Ebp1 shows that these residues are situated at solvent exposed positions close to the highly basic loop1 ( 63 IFKKEKEMK 71 ; Figure 5A); this suggests that, although loop1 has no demonstrated role in RNA binding (Figure 2), it may contribute to a bipartite nucleolar localisation signal.…”

Section: Discussionmentioning

confidence: 99%

Structural insights into the transcriptional and translational roles of Ebp1

Monie¹,

Perrin²,

Birtley³

et al. 2007

EMBO J

113

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The ErbB3-binding protein 1 (Ebp1) is an important regulator of transcription, affecting eukaryotic cell growth, proliferation, differentiation and survival. Ebp1 can also affect translation and cooperates with the polypyrimidine tract-binding protein (PTB) to stimulate the activity of the internal ribosome entry site (IRES) of foot-and-mouth disease virus (FMDV). We report here the crystal structure of murine Ebp1 (p48 isoform), providing the first glimpse of the architecture of this versatile regulator. The structure reveals a core domain that is homologous to methionine aminopeptidases, coupled to a C-terminal extension that contains important motifs for binding proteins and RNA. It sheds new light on the conformational differences between the p42 and p48 isoforms of Ebp1, the disposition of the key protein-interacting motif ( 354 LKALL 358 ) and the RNA-binding activity of Ebp1. We show that the primary RNA-binding site is formed by a Lys-rich motif in the C terminus and mediates the interaction with the FMDV IRES. We also demonstrate a specific functional requirement for Ebp1 in FMDV IRES-directed translation that is independent of a direct interaction with PTB.

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Section: Discussionmentioning

confidence: 99%

Structural insights into the transcriptional and translational roles of Ebp1

Monie¹,

Perrin²,

Birtley³

et al. 2007

EMBO J

113

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show abstract

“…We have identified a region of the protein that is necessary for nucleolar localization and rich in the positively charged amino acids lysine and arginine. Some nucleolar targeting sequences rich in positively charged amino acids have been found to mediate interactions with the RNA-rich environment of the nucleolus [41]. It is possible that G2E3 may interact with RNA within the nucleolus and that this is what mediates its nucleolar localization.…”

Section: Discussionmentioning

confidence: 99%

G2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization

Brooks

Banerjee

Crawford

2007

Experimental Cell Research

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G2E3 was originally described as a G2/M-specific gene with DNA damage responsive expression. The presence of a conserved HECT domain within the carboxy-terminus of the protein indicated that it likely functions as an ubiquitin ligase or E3. Although HECT domains are known to function in this capacity for many proteins, we demonstrate that a portion of the HECT domain from G2E3 plays an important role in the dynamic subcellular localization of the protein. We have shown that G2E3 is a nucleo-cytoplasmic shuttling protein with nuclear export mediated by a novel nuclear export domain that functions independently of CRM1. In full-length G2E3, a separate region of the HECT domain suppresses the function of the NES. Additionally, G2E3 contains a nucleolar localization signal (NoLS) in its amino terminus. Localization of G2E3 to the nucleolus is a dynamic process, and the protein delocalizes from the nucleolus rapidly after DNA damage. Cell cycle phase-specific expression and highly regulated subcellular localization of G2E3 suggest a possible role in cell cycle regulation and the cellular response to DNA damage.

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“…Taken together, these results indicate that the nucleolartargeting motif is located between amino acids 796 and 847. Indeed, close inspection of this region of myosin Vb reveals an 11 residue motif that closely resembles a region of the RNA binding nucleolar protein Nop25 [Fujiwara et al, 2006]. Myosin Vb truncation mutants fused to the much smaller Xpress tag display the same localisation pattern demonstrating that the GFP tag is not influencing the distribution of these constructs (data not shown).…”

Section: An Arginine-rich Region Targets Myosin Vb To Nucleolimentioning

confidence: 88%

“…Calmodulin (CaM) is a well established resident of the nucleus and nucleoli, where it has been implicated in functions such as mRNA splicing and ribosome biogenesis [Agell et al, 1998]. Interestingly, a region of the myosin Vb IQ motif 2 displays significant homology to a short domain that is essential for the nucleolar localisation of human Nop25 [Fujiwara et al, 2006] (Fig. 6F).…”

Section: Discussionmentioning

confidence: 99%

Myosin Vb localises to nucleoli and associates with the RNA polymerase I transcription complex

Lindsay

McCaffrey

2009

Cell Motil. Cytoskeleton

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It is becoming increasingly clear that the mammalian class V myosins are involved in a wide range of cellular processes such as receptor trafficking, mRNA transport, myelination in oligodendrocytes and cell division. Using paralog-specific antibodies, we observed significant nuclear localisation for both myosin Va and myosin Vb. Myosin Vb was present in nucleoli where it co-localises with RNA polymerase I, and newly synthesised ribosomal RNA (rRNA), indicating that it may play a role in transcription. Indeed, its nucleolar pattern was altered upon treatment with RNA polymerase I inhibitors. In contrast, myosin Va is largely excluded from nucleoli and is unaffected by these inhibitors. Myosin Vb was also found to physically associate with RNA polymerase I and actin in co-immunoprecipitation experiments. We propose that myosin Vb serves a role in rRNA transcription.

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Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25

Cited by 19 publications

References 26 publications

Structural insights into the transcriptional and translational roles of Ebp1

Structural insights into the transcriptional and translational roles of Ebp1

G2E3 is a nucleo-cytoplasmic shuttling protein with DNA damage responsive localization

Myosin Vb localises to nucleoli and associates with the RNA polymerase I transcription complex

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