Purification and characterization of seven chloroplast ribosomal proteins: evidence that organelle ribosomal protein genes are functional and that NH2-terminal processing occurs via multiple pathways in chloroplasts
✍ Scribed by J. Schmidt; E. Herfurth; A. R. Subramanian
- Book ID
- 104618786
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 538 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0167-4412
No coin nor oath required. For personal study only.
✦ Synopsis
Putative genes for 21 ribosomal proteins (RPs) have been identified in the chloroplast DNA of four plants by nucleotide sequencing and homology comparison but few of the gene products have been characterized. Here we report the purification and N-terminal sequencing of seven proteins from the spinach chloroplast ribosome. The data show them to be the homologues ofEscheriehia coli RPs L20, L32, L33, L36, $12, S16 and S19, and thus support the view that their genes identified in the chloroplast DNA represent functional genes. The initiating methionine residue was not detected in the mature protein in most cases but it was present in S 16, indicating that only the formyl group is removed in this case. This result and the previously reported finding of N-methyl alanine at the N-terminus of chloroplast L2 indicate the existence of multiple N-terminal processing pathways in the chloroplast.