The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeiana (bullfrog)

Chang, Chi Fon; Chen, Chinpan; Chen, Yi Cheng; Hom, Kellie; Huang, Rong; Huang, Tai Huang

doi:10.1006/jmbi.1998.2082

Cited by 25 publications

(13 citation statements)

References 52 publications

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“…In this search, we found only two structures~CSD codes DEGXAO and MGCUS! fulfilling this requirement and, interestingly, in both cases sulfate and guanine are linked by two hydrogen bonds as observed in RNaseA-UpG as well as in the other RNase complexes with guanine-containing nucleotides~Aguilar et al., 1992;Lisgarten et al, 1995;Chang et al, 1998;Vitagliano et al, 1999!. A similar search was repeated looking for structures containing guanine and the monoanionic phosphate of nucleotides. In this case, 48 structures were found, and in 18 cases the phosphate is directly bound to the guanine.…”

Section: Interactions Of Guanine With Sulfate and Phosphate In Small mentioning

confidence: 99%

“…Although the biological significance of retro-binding is still unclear, it has been shown that its occurrence is not restricted to RNase A. Indeed, retro-binding has been found in other members of the pancreatic-like ribonuclease superfamilỹ Chang et al, 1998!, including bovine seminal ribonuclease, which is endowed with special biological functions~Vitagliano et al, 1999!.…”

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confidence: 99%

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Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

et al. 2000

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Guanine-containing mono-and dinucleotides bind to the active site of ribonuclease A in a nonproductive modẽ retro-binding!~Aguilar CF, Thomas PJ, Mills A, Moss DS, Palmer RA, 1992, J Mol Biol 224:265-267!. Guanine binds to the highly specific pyrimidine site by forming hydrogen bonds with Thr45 and with the sulfate anion located in the P1 site. To investigate the influence of the anion present in the P1 site on retro-binding, we determined the structure of two new complexes of RNase A with uridylyl~29,59!guanosine obtained by soaking two different forms of pre-grown RNase A crystals. In one case, RNase A was crystallized without removing the sulfate anion strongly bound to the active site; in the other, the protein was first equilibrated with a basic solution to displace the anion from the P1 site. The X-ray structures of the complexes with and without sulfate in P1 were refined using diffraction data up to 1.8 Å~R-factor 0.192! and 2.0 Å~R-factor 0.178!, respectively. The binding mode of the substrate analogue to the protein differs markedly in the two complexes. When the sulfate is located in P1, we observe retro-binding; whereas when the anion is removed from the active site, the uridine is productively bound at the B1 site. In the productive complex, the electron density is very well defined for the uridine moiety, whereas the downstream guanine is disordered. This finding indicates that the interactions of guanine in the B2 site are rather weak and that this site is essentially adenine preferring. In this crystal form, there are two molecules per asymmetric unit, and due to crystal packing, only the active site of one molecule is accessible to the ligand. Thus, in the same crystal we have a ligand-bound and a ligand-free RNase A molecule. The comparison of these two structures furnishes a detailed and reliable picture of the structural alterations induced by the binding of the substrate. These results provide structural information to support the hypotheses on the role of RNase A active site residues that have recently emerged from site-directed mutagenesis studies.

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Section: Interactions Of Guanine With Sulfate and Phosphate In Small mentioning

confidence: 99%

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confidence: 99%

Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

et al. 2000

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“…In the feo operon, feoC is downstream of feoB. A multiple alignment of various bacterial FeoC amino acid sequences shows that they possess four conserved cysteine residues with a consensus sequence, CxxGxCKxCPx [4][5][6][7] C, that likely provides binding sites for iron in the form of an iron-sulfur ([Fe-S]) cluster (5). Therefore, FeoC is presumed to be an iron-sulfur-dependent regulator that directly controls transcription of the feo operon (5).…”

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Crystal Structure of the Klebsiella pneumoniae NFeoB/FeoC Complex and Roles of FeoC in Regulation of Fe ²⁺ Transport by the Bacterial Feo System

et al. 2012

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“…Thus, we considered that the caspase-9/-3 cascade is an important signal pathway in RC-6-induced cell death. RC-6, RC-RNase and onconase are all frog ribonucleases (22)(23)(24)(25). RC-RNase and onconase can induce caspase-9 and -3 activities in cancer cells; however, they cannot induce caspase-8 activity in cancer cells (31,36,38,54).…”

Section: Discussionmentioning

confidence: 99%

“…RC-RNase and onconase are frog ribonucleases purified from Rana catesbeiana and Rana pipiens, respectively. Both belong to the RNase A superfamily (22)(23)(24)(25). RC-RNase and onconase exert cytotoxic effects on various cancer cells such as hepatoma, cervical cancer, breast cancer, leukemia, mesothelioma, lung cancer, lymphoma, myeloma and prostate carcinoma (21,(26)(27)(28)(29)(30)(31).…”

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confidence: 99%

RC-6 ribonuclease induces caspase activation, cellular senescence and neuron-like morphology in NT2 embryonal carcinoma cells

et al. 2014

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Abstract.Frog ribonucleases have been demonstrated to have anticancer activities. However, whether RC-6 ribonuclease exerts anticancer activity on human embryonal carcinoma cells remains unclear. In the present study, RC-6 induced cytotoxicity in NT2 cells (a human embryonal carcinoma cell line) and our studies showed that RC-6 can exert anticancer effects and induce caspase-9 and -3 activities. Moreover, to date, there is no evidence that frog ribonuclease-induced cytotoxicity effects are related to cellular senescence. Therefore, our studies showed that RC-6 can increase p16 and p21 protein levels and induce cellular senescence in NT2 cells. Notably, similar to retinoic acid-differentiated NT2 cells, neuron-like morphology was found on some remaining live cells after RC-6 treatment. In conclusion, our study is the first to demonstrate that RC-6 can induce cytotoxic effects, caspase-9/-3 activities, cellular senescence and neuron-like morphology in NT2 cells.

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The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeiana (bullfrog)

Cited by 25 publications

References 52 publications

Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

Crystal Structure of the Klebsiella pneumoniae NFeoB/FeoC Complex and Roles of FeoC in Regulation of Fe ²⁺ Transport by the Bacterial Feo System

RC-6 ribonuclease induces caspase activation, cellular senescence and neuron-like morphology in NT2 embryonal carcinoma cells

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The solution structure of a cytotoxic ribonuclease from the oocytes of Rana catesbeiana (bullfrog)

Cited by 25 publications

References 52 publications

Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

Productive and nonproductive binding to ribonuclease A: X‐ray structure of two complexes with uridylyl(2′,5′)guanosine

Crystal Structure of the Klebsiella pneumoniae NFeoB/FeoC Complex and Roles of FeoC in Regulation of Fe 2+ Transport by the Bacterial Feo System

RC-6 ribonuclease induces caspase activation, cellular senescence and neuron-like morphology in NT2 embryonal carcinoma cells

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Crystal Structure of the Klebsiella pneumoniae NFeoB/FeoC Complex and Roles of FeoC in Regulation of Fe ²⁺ Transport by the Bacterial Feo System