Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and L23a, with unique histone-like amino-terminal extensions
Copyright policy )Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and L23a, with unique histone-like amino-terminal extensions
Poly(ADP-ribose) polymerase (PARP) is a nuclear enzyme that recognizes and binds to the nicks and ends of DNA, and catalyses successive ADP-ribosylation reactions. To clarify the function of PARP at the molecular level, we searched proteins which interact with PARP. In the auto-modification domain of PARP in Drosophila, there is a putative leucine-zipper motif which can interact with other protein molecules. To find interacting proteins we examined the auto-modification domain of Drosophila PARP, using the Far-Western screening method. From six independent cDNA clones isolated, we characterized two clones, PBP-3 and PBP-12. The predicted amino acid sequences from 109 to 269 of PBP-3 and from 184 to 312 of PBP-12 had more than 62% identities to mammalian L23a (rpl23a) and L22 (rpl22), the ribosomal proteins of the large subunit. This indicated that PBP-3 and PBP-12 are Drosophila homologues of L23a and L22, respectively. These Drosophila ribosomal protein L22 and L23a have additional Ala-, Lys- and Pro-rich sequences at the amino terminus, which have a resemblance to the carboxy-terminal portion of histone H1. Thus, Drosophila L22 and L23a might have two functions, namely the role of DNA-binding similar to histone H1 and the role of organizing the ribosome.
- University of Tsukuba Japan
Ribosomal Proteins, DNA, Complementary, Sequence Homology, Amino Acid, Blotting, Western, Molecular Sequence Data, RNA-Binding Proteins, Blotting, Northern, Molecular Probes, Mutagenesis, Site-Directed, Animals, Drosophila Proteins, Drosophila, Amino Acid Sequence, Cloning, Molecular, Poly(ADP-ribose) Polymerases, Protein Binding
Ribosomal Proteins, DNA, Complementary, Sequence Homology, Amino Acid, Blotting, Western, Molecular Sequence Data, RNA-Binding Proteins, Blotting, Northern, Molecular Probes, Mutagenesis, Site-Directed, Animals, Drosophila Proteins, Drosophila, Amino Acid Sequence, Cloning, Molecular, Poly(ADP-ribose) Polymerases, Protein Binding
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