Nucleoid proteins of pea chloroplasts: detection of a protein homologous to ribosomal protein

Basic proteins were isolated from purified pea chloroplast nucleoids by acid extraction. Using RP‐HPLC, the component composition of the basic proteins was studied. SDS‐PAGE of major HPLC‐fractions showed that the basic nucleoid proteins are heterogeneous with mol. masses of components from 17 to 30...

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Bibliographic Details
Published in:Biochemistry and molecular biology international 1999-05, Vol.47 (5), p.757-763
Main Authors: Oleskina, Yu.P, Yurina, N.P, Odintsova, T.I, Egorov, TS.A, Otto, A, Wittmann-Liebold, B, Odintsova, M.S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acid sequences
basic proteins
Cell Nucleus - metabolism
Chloroplast genome
Chloroplasts - physiology
Chromatography, High Pressure Liquid
Molecular Sequence Data
nicleoids
Nuclear Proteins - metabolism
nucleoproteins
Pisum sativum
Pisum sativum - physiology
Ribosomes - physiology
Time Factors
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Summary:Basic proteins were isolated from purified pea chloroplast nucleoids by acid extraction. Using RP‐HPLC, the component composition of the basic proteins was studied. SDS‐PAGE of major HPLC‐fractions showed that the basic nucleoid proteins are heterogeneous with mol. masses of components from 17 to 30 kDa. One polypeptide with mol. mass of 28 kDa (P28) was obtained by RP‐HPLC. The sequencing of three tryptic peptides of P28 (T6, T17, and T19) showed that they are homologous to the ribosomal protein L19 of Saccharomyces cerevisiae. The possible functional role of ribosomal proteins in chloroplast nucleoids is discussed.
ISSN:1039-9712
1521-6543
1521-6551
DOI:10.1080/15216549900201843