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 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.
Oleskina YuP
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Yurina
N P
NP
Odintsova
T I
TI
Egorov
T A
TA
Otto
A
A
Wittmann-Liebold
B
B
Odintsova
M S
MS
D000595:Amino Acid Sequence; D002467:Cell Nucleus / Q000378:metabolism; D002736:Chloroplasts / Q000502:physiology*; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism*; D018532:Pisum sativum / Q000502:physiology*; D012270:Ribosomes / Q000502:physiology*; D013997:Time Factors
D009687:Nuclear Proteins