Hanes J, Klaudiny J, von der Kammer H, Scheit K H
Max-Planck-Institut für biophysikalische Chemie, Abteilung Molekulare Biologie D-37077, Göttingen, Germany.
Biochem Biophys Res Commun. 1993 Dec 30;197(3):1223-8. doi: 10.1006/bbrc.1993.2607.
From a lambda UNI-ZAP XR cDNA library derived from poly(A)+RNA of human ovarian granulosa cells a cDNA clone pHG51 was isolated. Sequence analysis showed significant homology to the C-terminal region of rat ribosomal protein L8 cDNA. The 5'-end of the cDNA was completed by PCR with cloned total cDNA. Aligning of DNA sequences from PCR clones with the sequence of the pHG51 insert yielded the full-length cDNA. From the open reading frame of the cDNA an amino acid sequence for a polypeptide of 257 residues was derived, which was identical with rat ribosomal protein L8 and also possessed a high degree of identity to ribosomal proteins L8 of other species. It is therefore assumed that the characterized cDNA represents the mRNA of the human ribosomal protein L8. Southern analysis revealed that human ribosomal protein L8 is specified by multi copy genes.
