Vol. 40, No. 3, October 1996 BIOCHEMISTRY and MOLECULAR BIOLOGY INTERNATIONAL
Peges611-616
PRIMARY STRUCTURES AND SEQUENCE ANALYSIS OF HUMAN RIBOSOMAL
PROTEINS L39 AND $27 !
Stephen Kwok Wing Tsui, Simon Ming Yuen Lee, Kwok Pui Fung, Mary Miu Yee Waye,
Cheuk Yu Lee °
Department of Biochemistry,The Chinese UniversityofHong Kong, Shatin, N.T., Hong Kong
ReceivedJuly 24, 1996
SUMMARY
We report here the primary structures and sequence analysis of the human ribosomal protein
L39 (hRPL39) and $27 (hRPS27). The hRPL39 eDNA is 352 bp in size encoding a predicted
protein of 51 amino acids. The region KRRHWRRTKL near the earboxyl end is conserved
between human, rat, maize, C. elegans and yeast. The hRPS27 eDNA is 321 bp in size
encoding a deduced protein of 84 amino acids. When the deduced amino acid sequence of
hRPS27 was compared with that of rat ribosomal protein $27 and human metalloproteinstimulin-
1 (MPS-1), identity levels of 96.4% and 100% were obtained respectively. A potential
polyadenylation signal AACAAA is found in the MPS-1 eDNA but the more frequently used
AATAAA sequence is present in the hRPS27 eDNA. The carboxyl-terminal cyste'me
arrangement in hRPS27 is similar to the family of C4 zinc finger DNA-binding proteins.
Key words: Ribosomal protein L39; ribosomal protein $27; ribosomes; heart cDNAs; (Homo
sapiens).
Introduction
The mammalian ribosome is a supramolecular complex consisting of four different
subunits of RNA and approximately 80 different ribosomal proteins [1, 2]. Prokaryotes,
however, have only 50 ribosomal proteins [3, 4]. Most ribosomal protein genes are present at
7 to 20 copies in the genome [5], although some, such as rat ribosomal protein $5 [6] and
human ribosomal protein L37a [7], are present as single copy genes. In the search for novel
and previously uncharacterized genes, we initiated the expressed sequence tag lEST)
sequencing of human heart eDNA clones [8, 9]. Recently, we reported the sequencing and
characterization of the human ribosomal protein L29 [ 10]. Later, two novel eDNA clones with
DNA sequences resembling that of the rat ribosomal protein L39 (rRPL39) [11] and $27
(rRPS27) [12]. rRPL39 is located near ribosomal protein L12 in the 60S subunits and is found
to be cross-linked to the elongation factor 1 alpha [13]. By contrast, rRPS27 is located near
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Copyright © 1996 by Academic Press Australia.
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