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Nucleic Acids Research, 1991, Vol. 19, No. 23 6485-6490
© 1991

MOLECULAR BIOLOGY

Diversity of a ribonucleoprotein family in tobacco chlorplasts: two new chloroplast ribonucleoproteins and a phylogenetic tree of ten chloroplast RNA-binding domains

Lizhen Ye, Yuqing Li, Kaoru Fukami-Kobayashi1, Mitiko Go1, Tomokazu Konishi2, Akira Watanabe2 and Masahiro Sugiura

Center for Gene Research, Nagoya University Nagoya 464-01 Japan 1Department of Biology Japan 2Research Institute for Biochemical Regulation, Nagoya University Nagoya 464-01, Japan

Received August 23, 1991. Accepted November 8, 1991.

Two new ribonucleoproteins (RNPs) have been identified from a tobacco chloroplast lysate. These two proteins (cp29A and cp29B) are nuclear-encoded and have a less affinity to single-stranded DNA as compared with three other chloroplast RNPs (cp28, cp31 and cp33) previously isolated. DNA sequencing revealed that both contain two consensus sequence-type homologous RNA-binding domains (CS-RBDs) and a very acidic amino-terminal domain but shorter than that of cp28, cp31 and cp33. Comparison of cp29A and cp29B showed a 19 amino acid insertion in the region separating the two CS-RBDs in cp29B. This insertion results in three tandem repeats of a glycine-rich sequence of 10 amino acids, which is a novel feature in RNPs. The two proteins are encoded by different single nuclear genes and no alternatively spliced transcripts could be identified. We constructed a phylogenetic tree for the ten chloroplast CS-RBDs. These results suggest that there is a sizable RNP family in chloroplasts and the diversity was mainly generated through a series of gene duplications rather than through alternative pre-mRNA splicing. The gene for cp29B contains three introns. The first and second introns interrupt the first CS-RBD and the third intron does the second CS-RBD. The position of the first intron site is the same as that in the human hnRNP A1 protein gene.


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