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R J Martinez

Publications and source records attributed to R J Martinez.

32 records · Page 2Linked to original sources
PubMed1976

Amino acid sequence of flagellin of Bacillus subtilis 168. II. Tryptic peptides from maleylated flagellin.

Fifteen pure peptides, ranging in length from 2 to 141 residues, were isolated from the tryptic digest of maleylated flagellin. Studies of these peptides in conjunction with the data on the eight cyanogen bromide peptides described earlier (Chang, J. Y., DeLange, R. J., Shaper, J. H., and Glazer, A. N. (1976) J. Biol. Chem. 251, 695-700) established the order of three of the CNBr peptides at the NH2 terminus and of three at the COOH terminus of flagellin.

Amino Acid Sequence↗
PubMed1976

Bactericidal properties of human cell-free lymph.

The bactericidal properties of human cell-free lymph have been investigated. Gram-negative and gram-positive bacteria are susceptible to the killing action of lymph fluid. The colony-forming ability of Escherichia coli and Bacillus subtilis was reduced by 3 logs after 20 min of incubation with 10% (vol/vol) lymph. Salmonella and Listeria were less susceptible to killing. The presence of multiple killing factors in lymph showing different specificities for different bacterial cells was demonstrated.

Bacillus subtilis↗
PubMed1973

On the amino-acid sequence of flagellin from Bacillus subtilis 168: comparison with other bacterial flagellins.

A partial amino-acid sequence of Bacillus subtilis 168 flagellin is presented. The region of unassigned sequence in this 304-residue polypeptide chain spans residues 158-173. Comparison of the 27-residue aminoterminal CNBr peptide of B. subtilis 168 flagellin with that derived from the flagellin of the serologically unrelated strain of B. subtilis, W23, shows only three conservative substitutions, whereas the 16-residue carboxyl-terminal peptides derived from these flagellins were identical. The comparison of the very limited sequence information available on the flagellins of Salmonella and Proteus with that on B. subtilis indicates homology between these proteins.

Amino Acid Sequence↗
PubMed1972

Effect of proteolytic enzymes on bacterial flagella.

Sheared flagella of Salmonella typhimurium strains SL 870 (Nml(+)Fla(+)) and SL 871 (Nml(-)Fla(+)) were found to be susceptible to proteolytic digestion by trypsin, chymotrypsin, and Pronase. The rate of tryptic digestion was similar for the epsilon-N-methyllysine-containing and the nonmethylated flagella. Thin fibers, which appeared to originate from only one end of the flagellar filament, were formed upon trypsin digestion. The fibers were not dissociated at extremes of pH or upon heating. The amino acid composition of the purified fibers was very different from that of intact Salmonella flagellin, and the fibers did not cross-react with antiflagellin or antiflagellar antiserum. The possible significance of these findings is discussed in relation to the flagellar structure.

Amino Acids↗
PubMed1971

Methylation of the flagellin of Salmonella typhimurium.

The methylation of endogenous proteins by Salmonella typhimurium SL 870 was investigated in cell-free extracts by using S-adenosylmethionine as methyl donor. Several lines of evidence are presented which suggest that one of the methylated products is the protein flagellin. Mutant strains of SL 870 (nml(-)fla(+) and nml(+)fla(-)) were also found to synthesize epsilon-N-methyl-lysine. It is proposed that S. typhimurium possesses at least two genes specifying different methylating enzymes. One gene product is a flagellin-specific methylating enzyme, whereas the other gene(s) codes for enzymes that methylate one or more other cell proteins.

Acrylates↗
PubMed1969

Antigenic heterology between flagellin and flagella of Bacillus subtilis.

The antigenic properties of Bacillus subtilis flagella and periodate-treated flagellin were compared by using immobilization-inhibition and diethylaminoethyl cellulose binding assay. The results suggest that there are both unique and cross-reactive antibodies elicited by B. subtilis flagella and flagellin.

Antigens↗
PubMed1968

Primary adsorption site of phage PBS1: the flagellum of Bacillus subtilis.

The adsorption of Bacillus subtilis phage PBS1 was studied, and it was demonstrated that the primary adsorption site for this phage is the flagellum of B. subtilis. The capacity of flagella to function for motility may be lost without the loss of their capacity to adsorb the phage and permit infection. Deoxyribonucleic acid injection by the phage is inhibited by cyanide, suggesting the requirement for cellular energy in the infection process.

Adsorption↗
PubMed1966

Formation of bacterial flagella. I. Demonstration of a functional flagellin pool in spirillum serpens and bacillus subtilis.

Martinez, R. J. (University of California, Los Angeles), and E. Z. Gordee. Formation of bacterial flagella. I. Demonstration of a functional flagellin pool in Spirillum serpens and Bacillus subtilis. J. Bacteriol. 91:870-875. 1966-Exponentially growing cultures of Spirillum serpens and Bacillus subtilis regained motility and flagella within one generation after mechanical deflagellation. Regeneration of flagella occurred in both cultures in the presence of chloramphenicol at concentrations shown to inhibit flagellin synthesis. Cells labeled with C(14)-amino acids regenerated radioactive flagella in the presence of chloramphenicol. A conditional mutant of S. serpens (T-45) was isolated. This strain did not produce flagella when grown at 45 C, but formed the organelles upon temperature shift to 30 C, even in the presence of chloramphenicol. A reduction of intracellular antibody-precipitable flagellin counts in labeled S. serpens T-45 occurred concomitant with the generation of flagella at 30 C. The data suggest that the flagella of S. serpens and B. subtilis are formed from a pool of intracellular flagellin proteins.

Amino Acids↗