1990
DOI: 10.1016/0168-9452(90)90180-v
|View full text |Cite
|
Sign up to set email alerts
|

Chloroplast ribosomal proteins and their genes

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
24
0

Year Published

1991
1991
1998
1998

Publication Types

Select...
5
4

Relationship

0
9

Authors

Journals

citations
Cited by 43 publications
(24 citation statements)
references
References 77 publications
0
24
0
Order By: Relevance
“…Chloroplast 70S ribosomes contain about 60 different protein components (14,34,67,103), several more protein species than those in E. coli ribosomes (21 proteins in the 30S subunit and 34 proteins in the 50S subunit). In land plant chloroplasts, one third of the ribosomal proteins are encoded by ctDNA and the remaining two thirds are encoded in the nuclear genome.…”
Section: Ribosomal Protein Gene Clustersmentioning
confidence: 99%
“…Chloroplast 70S ribosomes contain about 60 different protein components (14,34,67,103), several more protein species than those in E. coli ribosomes (21 proteins in the 30S subunit and 34 proteins in the 50S subunit). In land plant chloroplasts, one third of the ribosomal proteins are encoded by ctDNA and the remaining two thirds are encoded in the nuclear genome.…”
Section: Ribosomal Protein Gene Clustersmentioning
confidence: 99%
“…3) soundly reflects the evolution of the species and organelles under study, explanations must be sought in the evolution of 16S rRNA genes which may account for the data. Aside from the problems of fluctuating GC content in bacterial evolution (Muto and Osawa 1987), one may recall that ribosomal RNAs evolve in the structural context of roughly 60 ribosomal proteins, about two-thirds of which are encoded by the nucleus in higher plants and green algae (Christopher et al 1988;Mache 1990;Subramanian et al 1991). Moreover, plastid ribosomes possess a number of unique features which their counterparts in free-living prokaryotes do not (Zhou and Mache 1989;Subramanian et al 1991).…”
Section: Origins Of Plastidsmentioning
confidence: 99%
“…After being centrifuged at 3,000 x g for 10 min, nuclei were lysed with buffer III (110 mM KCI, After being incubated at 4°C for 30 min, the proteins were collected by centrifugation at 10,000 x g for 15 min. The pellets were resuspended in a minimal volume of buffer IV (40 mM KCI, 25 Fig. 8), was labelled with Klenow enzyme at the BamHI site.…”
mentioning
confidence: 99%