Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses‐ A Review

Ranjbar, Bijan; Gill, Pooria

doi:10.1111/j.1747-0285.2009.00847.x

Cited by 545 publications

(382 citation statements)

References 175 publications

(268 reference statements)

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“…The CD spectra of the ICP27 N-terminal 160 amino acids (Fig. 5A) were consistent with a protein in a random-coil conformation due to the shape of the CD curve (31).…”

Section: Resultsmentioning

confidence: 61%

Three Arginine Residues within the RGG Box Are Crucial for ICP27 Binding to Herpes Simplex Virus 1 GC-Rich Sequences and for Efficient Viral RNA Export

Corbin-Lickfett¹,

Souki²,

Cocco

et al. 2010

J Virol

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ICP27 is a multifunctional protein that is required for herpes simplex virus 1 mRNA export. ICP27 interacts with the mRNA export receptor TAP/NXF1 and binds RNA through an RGG box motif. Unlike other RGG box proteins, ICP27 does not bind G-quartet structures but instead binds GC-rich sequences that are flexible in structure. To determine the contribution of arginines within the RGG box, we performed in vitro binding assays with N-terminal proteins encoding amino acids 1 to 160 of wild-type ICP27 or arginine-to-lysine substitution mutants. The R138,148,150K triple mutant bound weakly to sequences that were bound by the wild-type protein and single and double mutants. Furthermore, during infection with the R138,148,150K mutant, poly(A) ؉ RNA and newly transcribed RNA accumulated in the nucleus, indicating that viral RNA export was impaired. To determine if structural changes had occurred, nuclear magnetic resonance (NMR) analysis was performed on N-terminal proteins consisting of amino acids 1 to 160 from wild-type ICP27 and the R138,148,150K mutant. This region of ICP27 was found to be highly flexible, and there were no apparent differences in the spectra seen with wild-type ICP27 and the R138,148,150K mutant. Furthermore, NMR analysis with the wild-type protein bound to GC-rich sequences did not show any discernible folding. We conclude that arginines at positions 138, 148, and 150 within the RGG box of ICP27 are required for binding to GC-rich sequences and that the N-terminal portion of ICP27 is highly flexible in structure, which may account for its preference for binding flexible sequences.The herpes simplex virus 1 (HSV-1) protein ICP27 is a multifunctional regulatory protein that is required for productive viral infection. ICP27 interacts with a number of cellular proteins, and it binds RNA (35). One of the functions that ICP27 performs is to escort viral mRNAs from the nucleus to the cytoplasm for translation (2,3,5,10,13,21,34). ICP27 binds viral RNAs (5, 34) and interacts directly with the cellular mRNA export receptor TAP/NXF1 (2, 21), which is required for the export of HSV-1 mRNAs (20,21). ICP27 also interacts with the export adaptor proteins Aly/REF (2,3,23) and UAP56 (L. A. Johnson, H. Swesey, and R. M. Sandri-Goldin, unpublished results), which form part of the TREX complex that binds to the 5Ј end of mRNA through an interaction with CBP80 (26, 32, 41). Aly/REF does not appear to bind viral RNA directly (3), and it is not essential for HSV-1 RNA export based upon small interfering RNA (siRNA) knockdown studies (20), but it contributes to the efficiency of viral RNA export (3, 23). ICP27 also interacts with the SR splicing proteins SRp20 and 9G8 (11,36), which have been shown to shuttle between the nucleus and the cytoplasm (1). SRp20 and 9G8 have also been shown to facilitate the export of some cellular RNAs (16,17,27) by binding RNA and interacting with TAP/ NXF1 (14,16,18). The knockdown of SRp20 or 9G8 adversely affects HSV-1 replication and specifically results in a nuclear accumulation of new...

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“…The CD spectra of the ICP27 N-terminal 160 amino acids (Fig. 5A) were consistent with a protein in a random-coil conformation due to the shape of the CD curve (31).…”

Section: Resultsmentioning

confidence: 61%

Three Arginine Residues within the RGG Box Are Crucial for ICP27 Binding to Herpes Simplex Virus 1 GC-Rich Sequences and for Efficient Viral RNA Export

Corbin-Lickfett¹,

Souki²,

Cocco

et al. 2010

J Virol

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“…We determined the structural property of HKPLP using CD spectroscopy and the absorption curve presented v-shaped spectra indicating b-sheet, 22 as shown in Figure 5. …”

Section: Spectroscopymentioning

confidence: 99%

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Sun

Jing

et al. 2012

J Antibiot

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A novel gene encoding 55 amino-acid residues has been identified from the brooding pouch cDNA library of Hippocampus kuda Bleeker. The deduced amino-acid sequence is highly homologous to several pleurocidin-like peptides from the winter flounder and comprises a signal peptide, a pro-peptide and a mature peptide. The glycine-rich mature peptide, designated HKPLP, contains 24 amino-acid residues and has been synthesized by solid-phase peptide synthesis. The purified HKPLP exhibits antimicrobial activity against several Gram-positive and Gram-negative bacterial strains at low concentrations (MIC 1.5-7.5 lM). Thermal stability assay data show good heat stability. CD spectroscopy experiments indicate that the dominant contents are anti-parallel and parallel sheets, which may have b-sheet or b-strand motif. It is inferred that HKPLP participates in the host defense during egg fertilization and embryo development as an antimicrobial peptide in brooding pouch.

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“…The signal at that wavelength is then recorded continuously as the temperature is raised. CD is often used to investigate the effect of solution pH, buffers, and additives such as sugars, amino acids or salts on thermal stability [33]. In this study, the ellipticity value at 218 nm was chosen as the parameter describing the global secondary structure variations of the protein.…”

Section: International Journal Ofmentioning

confidence: 99%

Indirect Evidence for Self Association of Muscle Fatty Acid Binding Protein from Locusta migratoria

Hai¹,

Kizilbash²,

Zaidi³

et al. 2014

IJBBB

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Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses‐ A Review

Cited by 545 publications

References 175 publications

Three Arginine Residues within the RGG Box Are Crucial for ICP27 Binding to Herpes Simplex Virus 1 GC-Rich Sequences and for Efficient Viral RNA Export

Three Arginine Residues within the RGG Box Are Crucial for ICP27 Binding to Herpes Simplex Virus 1 GC-Rich Sequences and for Efficient Viral RNA Export

Identification, synthesis and characterization of a novel antimicrobial peptide HKPLP derived from Hippocampus kuda Bleeker

Indirect Evidence for Self Association of Muscle Fatty Acid Binding Protein from Locusta migratoria

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