NDLI: Ornithine decarboxylase inThermus thermophilus: An RNA-associated enzyme

Content Provider	Springer Nature Link
Author	Pantazaki, A. A. Liakopoulou Kyriakides, M. Kyriakidis, D. A.
Copyright Year	1997
Abstract	Ornithine decarboxylase (ODC) ofThermus thermophilus is associated with the nucleoid protein fraction. Analysis of this fraction by agarose gel electrophoresis and immunostaining revealed that ODC was bound to two groups of RNA-protein complexes. These two complexes of 1.5 and 0.6 kb in size disappeared from the gel by RNase A treatment or migrated to small molecular weight complexes by proteinase K treatment. Phenol extraction of either the nucleoid fraction or the eluted RNA-protein complexes from the agarose gel, shows that both contain the 0.56kb RNA. Both RNA-protein complexes contain the ODC protein (55 kDa) but their protein composition differs in at least six proteins. Extraction of the nucleoid fraction with H2SO4, indicates that ODC was present in the acid-soluble fraction, showing that it is a non-histone protein tightly bound to 0.56kb RNA. The purified ODC by various columns (∼140-fold), is close to homogeneity and still carries the 0.56kb RNA further explaining all the difficulties in the purification of this enzyme.
Starting Page	299
Ending Page	309
Page Count	11
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	13
Issue Number	3-4
e-ISSN	14382199
Language	English
Publisher	Springer-Verlag
Publisher Date	1997-01-01
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Amino acids Ornithine decarboxylase Thermus thermophilus RNA complex Analytical Chemistry Biochemical Engineering Life Sciences Biochemistry Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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