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1.
J Dent Res ; 81(12): 817-21, 2002 Dec.
Article in English | MEDLINE | ID: mdl-12454094

ABSTRACT

Ectopic calcification within joints has been reported in humans and rodents exhibiting mutations in genes that regulate the level of extracellular pyrophosphate, e.g., ank and PC-1; however, periodontal effects of these mutations have not previously been examined. These initial studies using ank and PC-1 mutant mice were done to see if such mineral deposition and resulting ankylosis were occurring in the periodontium as well. Surprisingly, results indicated the absence of ankylosis; however, a marked increase in cementum formation on the root surfaces of fully developed teeth of these mutant mice was noted. Examination of ank mutant mice at earlier ages of tooth root formation indicated that this striking observation is apparent from the onset of cementogenesis. These findings suggest that cells within the periodontal region are highly responsive to changes in phosphate metabolism. This information may prove valuable in attempts to design successful therapies for regenerating periodontal tissues.


Subject(s)
Cementogenesis/genetics , Dental Cementum/metabolism , Diphosphates/metabolism , Animals , Membrane Proteins/genetics , Mice , Mice, Mutant Strains , Mutation , Phosphate Transport Proteins , Phosphoric Diester Hydrolases/genetics , Pyrophosphatases/genetics , Tooth Root/growth & development
2.
Nucleic Acids Res ; 25(23): 4778-85, 1997 Dec 01.
Article in English | MEDLINE | ID: mdl-9365256

ABSTRACT

A single base change in the helicase superfamily 1 domain of the yeast Saccharomyces cerevisiae SEN1 gene results in a heat-sensitive mutation that alters the cellular abundance of many RNA species. We compared the relative amounts of RNAs between cells that are wild-type and mutant after temperature-shift. In the mutant several RNAs were found to either decrease or increase in abundance. The affected RNAs include tRNAs, rRNAs and small nuclear and nucleolar RNAs. Many of the affected RNAs have been positively identified and include end-matured precursor tRNAs and the small nuclear and nucleolar RNAs U5 and snR40 and snR45. Several small nucleolar RNAs co-immunoprecipitate with Sen1 but differentially associate with the wild-type and mutant protein. Its inactivation also impairs precursor rRNA maturation, resulting in increased accumulation of 35S and 6S precursor rRNAs and reduced levels of 20S, 23S and 27S rRNA processing intermediates. Thus, Sen1 is required for the biosynthesis of various functionally distinct classes of nuclear RNAs. We propose that Sen1 is an RNA helicase acting on a wide range of RNA classes. Its effects on the targeted RNAs in turn enable ribonuclease activity.


Subject(s)
Fungal Proteins/genetics , RNA Processing, Post-Transcriptional , RNA, Fungal/metabolism , RNA, Small Nuclear/metabolism , Saccharomyces cerevisiae/genetics , Antibodies/immunology , DNA Helicases , Fungal Proteins/immunology , Fungal Proteins/metabolism , Mutagenesis , RNA Helicases , RNA Precursors/metabolism , RNA Splicing , RNA, Messenger/metabolism , RNA, Ribosomal/metabolism , Saccharomyces cerevisiae Proteins
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