Solution Structure of the Cytotoxic RNase 4 from Oocytes of Bullfrog Rana catesbeiana

Hsu, Chun‐Hua; Liao, You‐Di; Pan, Yun‐Ru; Chen, Lih-Woan; Wu, Shih‐Hsiung; Leu, Ying-Jen; Chen, Chinpan

doi:10.1016/s0022-2836(02)01472-9

Cited by 17 publications

(11 citation statements)

References 48 publications

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“…The NMR spectra were acquired on Bruker AV600 and AV800 spectrometers equipped with 5-mm triple resonance cryoprobe and single-axis pulsed-field gradient at 310 K as described [9], [32], [33]. NMR data were collected in Shigemi tubes with 1-mM protein samples in 20 mM Na 3 PO 4 , 50 mM NaCl, 10% D 2 O at pH 6.5.…”

Section: Methodsmentioning

confidence: 99%

Solution Structure of the Oncogenic MIEN1 Protein Reveals a Thioredoxin-Like Fold with a Redox-Active Motif

et al. 2012

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The novel tumor biomarker MIEN1, identified by representational difference analysis, is overexpressed in breast cancer and prostate cancer. MIEN1 is considered an oncogenic protein, because MIEN1 overexpression functionally enhances migration and invasion of tumor cells via modulating the activity of AKT. However, the structure and molecular function of MIEN1 is little understood. Here, we report the solution structure of MIEN1, which adopts a thioredoxin-like fold with a redox-active motif. Comparison of backbone chemical shifts showed that most of the residues for both oxidized and reduced MIEN1 possessed the same backbone conformation, with differences limited to the active motif and regions in proximity. The redox potential of this disulfide bond was measured as −225 mV, which compares well with that of disulfides for other thioredoxin-like proteins. Overall, our results suggest that MIEN1 may have an important regulatory role in phosphorylation of AKT with its redox potential.

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Section: Methodsmentioning

confidence: 99%

Solution Structure of the Oncogenic MIEN1 Protein Reveals a Thioredoxin-Like Fold with a Redox-Active Motif

et al. 2012

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“…Typical homonuclear and heteronuclear NMR spectra (17,18) were recorded at 310 K on a Bruker Avance-800, Avance-600 or AMX-500 spectrometer with use of cryogenic triple-resonance probes with z -axis pulse-field gradient capability, essentially as described (19). …”

Section: Methodsmentioning

confidence: 99%

The DNA-recognition fold of Sso7c4 suggests a new member of SpoVT-AbrB superfamily from archaea

Hsu

Wang

2011

Nucleic Acids Research

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Organisms growing at elevated temperatures face the challenge of maintaining the integrity of their genetic materials. Archaea possess unique chromatin proteins for gene organization and information processing. We present the solution structure of Sso7c4 from Sulfolobus solfataricus, which has a homodimeric DNA-binding fold forming a swapped β-loop-β ‘Tai-Chi’ topology. The fold is reminiscent of the N-terminal DNA-binding domain of AbrB and MazE. In addition, several amide resonances in the heteronuclear single quantum coherence spectra of Sso7c4 are shifted and broadened with the addition of small amounts of duplex DNA oligomers. The locations of the corresponding amides in the Sso7c4 structure define its DNA-interacting surface. NMR spectra of DNA titrated with the protein further indicated that Sso7c4 interacts with DNA in the major groove. Taken together, a plausible model for the Sso7c4–DNA complex is presented, in which the DNA double helix is curved around the protein dimer.

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“…The normal and uniformly 15 N/ 13 Clabeled pRNase 3 and mqRNase 3 were produced using the E. coli expression system, refolded from inclusion bodies and purified as described. 12,29 The purified refolded RC-RNase 3 was further dialyzed against 20 mM sodium phosphate (pH 7.0), and incubated at 37 8C for the conversion of N-terminal glutamine to pyroglutamate. SDS-PAGE and mass spectrometry were carried out to confirm the purity and identity of the proteins.…”

Section: Preparation Of Ribonucleasesmentioning

confidence: 99%

“…GdnHCl-induced protein denaturation was monitored by CD and fluorescence as described. 12 The curves were fit and analyzed using SigmaPlot 8.02 (SPSS Inc.)…”

Section: Preparation Of Ribonucleasesmentioning

confidence: 99%

“…9 However, the cytotoxicities of frog ribonucleases are dramatically reduced if the N-terminal Pyr1 residue is replaced. [10][11][12] In addition, compared to the other R. catesbeiana ribonucleases, RC-RNase 3 (RNase 3) shows relatively broad base specificity and low catalytic activity, but with similar cytotoxicity toward tumor cells. More interestingly, it has the lowest optimal pH (4.5-5.0) for catalytic activity.…”

Section: Introductionmentioning

confidence: 99%

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Roles of N-terminal Pyroglutamate in Maintaining Structural Integrity and pKa Values of Catalytic Histidine Residues in Bullfrog Ribonuclease 3

Lou

Huang

Pan

et al. 2006

Journal of Molecular Biology

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Solution Structure of the Cytotoxic RNase 4 from Oocytes of Bullfrog Rana catesbeiana

Cited by 17 publications

References 48 publications

Solution Structure of the Oncogenic MIEN1 Protein Reveals a Thioredoxin-Like Fold with a Redox-Active Motif

Solution Structure of the Oncogenic MIEN1 Protein Reveals a Thioredoxin-Like Fold with a Redox-Active Motif

The DNA-recognition fold of Sso7c4 suggests a new member of SpoVT-AbrB superfamily from archaea

Roles of N-terminal Pyroglutamate in Maintaining Structural Integrity and pKa Values of Catalytic Histidine Residues in Bullfrog Ribonuclease 3

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