The Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus

Turner, Catherine F.; Moore, Peter B.

doi:10.1016/j.jmb.2003.11.018

Cited by 7 publications

(5 citation statements)

References 27 publications

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“…These observations suggest that almost all ribosomal proteins are likely to be intrinsically disordered in isolation but fold to a different degree upon the ribosome formation . This hypothesis is in agreement with the earlier experimental studies, which showed that many individual ribosomal proteins do not possess ordered structure in their nonbound forms or at least contain long disordered regions. ,− Further support to this idea came from the comprehensive bioinformatics analysis of 3411 ribosomal proteins from 32 species . This analysis revealed that the vast majority of ribosomal proteins are intrinsically disordered, and that intrinsic disorder is very important for various biological functions of these important RNA-binding proteins, being commonly used as means for the numerous interactions of any given ribosomal protein with its various binding partners of different nature, such as other ribosomal proteins, RNA, and proteins from the translational machinery.…”

Section: Illustrative Examples Of Pliable Proteinaceous Machinessupporting

confidence: 83%

Disordered Proteinaceous Machines

et al. 2014

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Section: Illustrative Examples Of Pliable Proteinaceous Machinessupporting

confidence: 83%

Disordered Proteinaceous Machines

et al. 2014

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“…RanBP1_WASP is a domain that is known to bind proline-rich sequences for protein-protein interaction (33). The L18 domain of L5 is homologous to the bacterial ribosomal protein L18, which is responsible for 5S rRNA-protein binding (34,35). Figure 5B shows that the addition of the L18 domain of L5 decreased the emission of the FRET interacting pair at 530 nm, suggesting that the L18 domain of L5 is involved in association with P34.…”

Section: Discussionmentioning

confidence: 99%

“…Figure 5B shows that the addition of the L18 domain of L5 decreased the emission of the FRET interacting pair at 530 nm, suggesting that the L18 domain of L5 is involved in association with P34. The L18 domain contains three ␣-helices and four-stranded ␤-sheets (35). Most of the residues involved in 5S rRNA binding are located on the face of the ␤-sheets (35).…”

Section: Discussionmentioning

confidence: 99%

“…The L18 domain contains three ␣-helices and four-stranded ␤-sheets (35). Most of the residues involved in 5S rRNA binding are located on the face of the ␤-sheets (35). It has been reported that the RRM can associate with other protein domains through their ␣-helices, and the interaction is stabilized by salt bridges or hydrophobic interactions (30,36,37).…”

Section: Discussionmentioning

confidence: 99%

“…It is known that the L18 domain of L5 is important for binding to 5S rRNA (35). Thus, domains of P34 and L5 for protein-protein and protein-5S rRNA interaction may be close to one another or overlap.…”

Section: Discussionmentioning

confidence: 99%

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Association of a Novel Preribosomal Complex in Trypanosoma brucei Determined by Fluorescence Resonance Energy Transfer

Wang¹,

Ciganda²,

Williams³

2013

Eukaryot Cell

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We have previously reported that the trypanosome-specific proteins P34 and P37 form a unique preribosomal complex with ribosomal protein L5 and 5S rRNA in the nucleoplasm. We hypothesize that this novel trimolecular complex is necessary for stabilizing 5S rRNA in Trypanosoma brucei and is essential for the survival of the parasite. In vitro quantitative analysis of the association between the proteins L5 and P34 is fundamental to our understanding of this novel complex and thus our ability to exploit its unique characteristics. Here we used in vitro fluorescence resonance energy transfer (FRET) to analyze the association between L5 and P34. First, we demonstrated that FRET can be used to confirm the association between L5 and P34. We then determined that the binding constant for L5 and P34 is 0.60 ؎ 0.03 M, which is in the range of protein-protein binding constants for RNA binding proteins. In addition, we used FRET to identify the critical regions of L5 and P34 involved in the protein-protein association. We found that the N-terminal APK-rich domain and RNA recognition motif (RRM) of P34 and the L18 domain of L5 are important for the association of the two proteins with each other. These results provide us with the framework for the discovery of ways to disrupt this essential complex.A frican trypanosomes are responsible for trypanosomiasis in humans and nagana in domestic animals. Trypanosoma brucei has a complicated life cycle that requires adaptation to life within a mammalian host and an insect vector, the tsetse fly (1). Throughout this life cycle, RNA binding proteins (RBPs) play the central roles in many adaptive processes, including regulation of gene expression and protein synthesis (2, 3), making them particularly important in this organism.RBPs play essential roles in the many aspects of ribosomal biogenesis. Ribosomal biogenesis in eukaryotes is an essential and conserved process that requires the processing and assembly of four rRNAs (18, 28, 5.8, and 5S rRNAs) with over 80 ribosomal proteins. Much of this process occurs in the nucleolus (4-6). However, unlike the other three rRNAs, 5S rRNA is independently transcribed by RNA polymerase III within the nucleoplasm and must be transported into the nucleolus by the L5 ribosomal protein (7,8). L5 is the only known eukaryotic ribosomal protein that forms a preribosomal L5-5S rRNA ribonucleoprotein (RNP) complex to stabilize and facilitate the trafficking of 5S rRNA to the nucleolus (7, 9, 10). Mutations in critical residues within L5 lead to loss of 5S rRNA and ribosomal biogenesis defects, indicating that it is essential to cell viability. T. brucei L5 is comprised of a predicted RanBP1_WASP domain in its N-terminal region, an L18 domain in the central region, and a C-terminal domain that possesses residues critical for 5S rRNA binding.Our laboratory has previously identified two trypanosomespecific RBPs, P34 and P37, which are essential for the viability of T. brucei (11). P34 and P37 are highly similar, the major difference between them being the pre...

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A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome

Peng

Oldfield

Xue

et al. 2013

Cell. Mol. Life Sci.

132

114

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Intrinsic disorder (i.e., lack of a unique 3-D structure) is a common phenomenon, and many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions constitute a significant part of all proteomes, and their functional repertoire is complementary to functions of ordered proteins. In fact, intrinsic disorder represents an important driving force for many specific functions. An illustrative example of such disorder-centric functional class is RNA-binding proteins. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 3,411 ribosomal proteins from 32 species. We show that many ribosomal proteins are intrinsically disordered or hybrid proteins that contain ordered and disordered domains. Predicted globular domains of many ribosomal proteins contain noticeable regions of intrinsic disorder. We also show that disorder in ribosomal proteins has different characteristics compared to other proteins that interact with RNA and DNA including overall abundance, evolutionary conservation, and involvement in protein-protein interactions. Furthermore, intrinsic disorder is not only abundant in the ribosomal proteins, but we demonstrate that it is absolutely necessary for their various functions.

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The Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus

Cited by 7 publications

References 27 publications

Disordered Proteinaceous Machines

Disordered Proteinaceous Machines

Association of a Novel Preribosomal Complex in Trypanosoma brucei Determined by Fluorescence Resonance Energy Transfer

A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome

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