Seminal RNase: a unique member of the ribonuclease superfamily

D’Alessio, Giuseppe; Donato, Alberto Di; Parente, Augusto; Piccoli, Renata

doi:10.1016/0968-0004(91)90042-t

Cited by 144 publications

(81 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We were surprised to observe a large difference in pH optimum (ϳ1.3 pH units) for catalysis by the native dimeric form of BSR and the artificial monomer. The dimeric structure of BSR is also necessary for its other putative biological functions, including its immunosuppressive and antitumor activity (22,46). The dimer is known to swap its N-terminal helices (69,70), thereby forming a chimeric active site that could have higher histidine pK a values.…”

Section: Discussionmentioning

confidence: 99%

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Eller

Lomax

Raines

2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: RNase 1 is an RNA-degrading enzyme conserved in mammals and with unknown biological function. Results: RNase 1 homologs in human and cow display different biochemical and biological properties, implying divergent physiology. Conclusion: Bovine brain ribonuclease, not RNase A, is the functional homolog of human RNase 1. Significance: Fundamental insight into the biology and evolution of human RNase 1 is attained from analyses of homologous proteins.

show abstract

Section: Discussionmentioning

confidence: 99%

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Eller

Lomax

Raines

2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…We have not determined whether the 85-and 110-kDa activity peaks represent distinct enzymes or multimeric complexes containing the ϳ39-kDa endonuclease. It would not be surprising if the endonuclease formed multimers with itself or with other proteins, because dimer/multimer formation is a common feature of many RNases (27)(28)(29)(30).…”

Section: Identification and Purification Of A Polysomal C-mycmentioning

confidence: 99%

Purification and Characterization of a Polysome-associated Endoribonuclease That Degrades c-myc mRNA in Vitro

Lee

Leeds

Ross

1998

Journal of Biological Chemistry

106

View full text Add to dashboard Cite

The regulation of mRNA half-lives is determined by multiple factors, including the activity of the messenger RNases (mRNases) responsible for destroying mRNA molecules. Previously, we used cell-free mRNA decay assays to identify a polysome-associated endonuclease that cleaves c-myc mRNA within the coding region. A similar activity has been solubilized and partially purified from a high salt extract of adult rat liver polysomes. Based on a correlation between protein and enzyme activity, the endonuclease is tentatively identified as a ϳ39-kDa protein. It cleaves the coding region stability determinant of c-myc mRNA with considerable specificity. Cleavages occur predominantly in an A-rich segment of the RNA. The endonuclease is resistant to RNase A inhibitors, sensitive to vanadyl ribonucleoside complex, and dependent on magnesium. In these and other respects, the soluble enzyme we have purified resembles the polysome-associated c-myc mRNase.

show abstract

“…The known biological functions of lactoferrin are the stimulation of DNA synthesis (200), the transport of iron through the fetal intestine (201), the modulation of the immune system (202,203), and bacteriostatic/bactericidal activities by chelating iron (204). Lactoferrin is believed to play a role in the uterus by one or more of the following mechanisms: as an iron reservoir (205), by maintaining uterine proliferation (206), by tissue remodeling through its intrinsic RNase activity (207)(208)(209), or by fighting infections through its bacteriostatic (194) and bacteriocidal (204) activities. (190) Tilapia (191) Tiger prawn (192) Blue crab (193) Like vitellogenin, lactoferrin is under the positive regulatory control of estrogen.…”

Section: Altered Steroid Hormone Homeostasis In Fishmentioning

confidence: 99%

Chronic Toxicity of Environmental Contaminants: Sentinels and Biomarkers

LeBlanc¹,

Bain²

1997

Environmental Health Perspectives

View full text Add to dashboard Cite

Due to the use of a limited number of species and subchronic exposures, current ecological hazard assessment processes can underestimate the chronic toxicity of environmental contaminants resulting in adverse responses of sentinel species. Several incidences where sentinel species have responded to the effects of chronic exposure to ambient levels of environmental contaminants are discussed, including the development of neoplasia in fish, immunosuppression in marine mammals, pseudohermaphrodism in invertebrates, teratogenicity in amphibians, and aberrations in the sexual development of fish and reptiles. Biomarkers of chronic toxicity, including DNA mutations, alterations in specific protein and mRNA levels, and perturbations in metabolism, are presented. The incorporation of appropriate surrogate species and biomarkers of chronic toxicity into standard toxicity characterizations is proposed as a means of significantly refining the ecological hazard assessment process. -Environ Health Perspect 105(Suppl 1): 65-80 (1997)

show abstract

Seminal RNase: a unique member of the ribonuclease superfamily

Cited by 144 publications

References 23 publications

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Bovine Brain Ribonuclease Is the Functional Homolog of Human Ribonuclease 1

Purification and Characterization of a Polysome-associated Endoribonuclease That Degrades c-myc mRNA in Vitro

Chronic Toxicity of Environmental Contaminants: Sentinels and Biomarkers

Contact Info

Product

Resources

About