» Articles » PMID: 110790

Localization of Low-molecular-weight Basic Proteins in Bacillus Megaterium Spores by Cross-linking with Ultraviolet Light

Overview
Journal J Bacteriol
Specialty Microbiology
Date 1979 Aug 1
PMID 110790
Citations 20
Authors
Affiliations
Soon will be listed here.
Abstract

Two low-molecular-weight basic proteins, termed A and B proteins, comprise about 15% of the protein of dormant spores of Bacillus megaterium. Irradiation of intact dormant spores with ultraviolet light results in covalent cross-linking of the A and B proteins to other spore macromolecules. The cross-linked A and B proteins are precipitated by ethanol and can be solubilized by treatment with deoxyribonuclease (75%) or ribonuclease (25%). Irradiation of complexes formed in vitro between deoxyribonucleic acid (DNA) or ribonucleic acid and a mixture of the low-molecular-weight basic proteins from spores also resulted in cross-linking of A and B proteins to nucleic acids. The dose-response curves for formation of covalent cross-links were similar for irradiation of both a protein-DNA complex in vitro and intact spores. However, if irradiation was carried out in vitro under conditions where DNA-protein complexes were disrupted, no covalent cross-links were formed. These data suggest that significant amounts of the low-molecular-weight basic proteins unique to bacterial spores are associated with spore DNA in vivo.

Citing Articles

Effects of carboxy-terminal modifications and pH on binding of a Bacillus subtilis small, acid-soluble spore protein to DNA.

Kosman J, Setlow P J Bacteriol. 2003; 185(20):6095-103.

PMID: 14526021 PMC: 225040. DOI: 10.1128/JB.185.20.6095-6103.2003.


Analysis of nucleoid morphology during germination and outgrowth of spores of Bacillus species.

Ragkousi K, Cowan A, Ross M, Setlow P J Bacteriol. 2000; 182(19):5556-62.

PMID: 10986261 PMC: 111001. DOI: 10.1128/JB.182.19.5556-5562.2000.


DNA stability and survival of Bacillus subtilis spores in extreme dryness.

Dose K, Gill M Orig Life Evol Biosph. 1995; 25(1-3):277-93.

PMID: 7708386 DOI: 10.1007/BF01581591.


Noninvolvement of the spore cortex in acquisition of low-molecular-weight basic proteins and UV light resistance during Bacillus sphaericus sporulation.

Setlow B, Hackett R, Setlow P J Bacteriol. 1982; 149(2):494-8.

PMID: 7056695 PMC: 216533. DOI: 10.1128/jb.149.2.494-498.1982.


Bacillus megaterium spore protease: purification, radioimmunoassay, and analysis of antigen level and localization during growth, sporulation, and spore germination.

Loshon C, Setlow P J Bacteriol. 1982; 150(1):303-11.

PMID: 6801023 PMC: 220114. DOI: 10.1128/jb.150.1.303-311.1982.


References
1.
Postemsky C, Dignam S, Setlow P . Isolation and characterization of Bacillus megaterium mutants containing decreased levels of spore protease. J Bacteriol. 1978; 135(3):841-50. PMC: 222455. DOI: 10.1128/jb.135.3.841-850.1978. View

2.
Setlow P . Purification and characterization of additional low-molecular-weight basic proteins degraded during germination of Bacillus megaterium spores. J Bacteriol. 1978; 136(1):331-40. PMC: 218665. DOI: 10.1128/jb.136.1.331-340.1978. View

3.
Setlow P, Primus G . Protein metabolism during germination of Bacillus megaterium spores. I. Protein synthesis and amino acid metabolism. J Biol Chem. 1975; 250(2):623-30. View

4.
Setlow P . Identification and localization of the major proteins degraded during germination of Bacillus megaterium spores. J Biol Chem. 1975; 250(20):8159-67. View

5.
Setlow P . Purification and properties of some unique low molecular weight basic proteins degraded during germination of Bacillus megaterium spores. J Biol Chem. 1975; 250(20):8168-73. View