Determination of the cross-linked residues in homo-dimerization of S19 ribosomal protein concomitant with exhibition of monocyte chemotactic activity.
When S19 ribosomal protein molecules are intermolecularly cross-linked by a transglutaminase-catalyzed reaction, the monocyte chemotactic activity is newly expressed. Heparin, at a concentration of 1 U/ml, greatly augmented the cross-linking reaction. This augmentation was due to binding affinity of S19 ribosomal protein to heparin. The major heparin-binding region of S19 ribosomal proteins was identified to Lys23-Lys-Ser-Gly-Lys-Leu-Lys29, using region-directed mutant proteins. The amino acid residues of S19 ribosomal protein used for the intermolecular cross-linkage were then determined by the peptide map analysis with amino acid sequencing and by the site-directed mutagenesis; Gln137 and Lys122 were used in the intermolecular cross-linkage.
Nishiura
H
H
Division of Molecular Pathology, Graduate School of Medical Sciences, Kumamoto University, Japan.
Tanase
S
S
Sibuya
Y
Y
Nishimura
T
T
Yamamoto
T
T
D000595:Amino Acid Sequence; D002122:Calcium Chloride / Q000494:pharmacology; D002634:Chemotaxis, Leukocyte / Q000187:drug effects*; D019281:Dimerization; D006493:Heparin / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D008969:Molecular Sequence Data; D009000:Monocytes / Q000276:immunology*; D016297:Mutagenesis, Site-Directed; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000494:pharmacology
D012269:Ribosomal Proteins; C040343:ribosomal protein S19; D006493:Heparin; D002122:Calcium Chloride