HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Setlow, P. Search for Related Content PubMed PubMed Citation Articles by Setlow, P. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 20, 8168-8173, Oct, 1975

Purification and properties of some unique low molecular weight basic proteins degraded during germination of Bacillus megaterium spores

P. Setlow

Two major proteins, termed proteins A and B, and one minor species, termed protein C, have been purified to homogeneity from dilute acid extracts of dormant spores of Bacillus megaterium. These three species comprise approximately 80% of the protein in the dilute acid extracts and account for 60 to 75% of the protein degraded during spore germination. All three proteins have low molecular weights (7,000 to 10,000), high isoelectric points (greater than 9.8), alanine as the NH2-terminal amino acid, are more hydrophilic than most proteins, and all lack cysteine, cystine, and tryptophan. In addition all three proteins are extremely sensitive to a wide variety of proteolytic enzymes, much more so than "average" proteins such as serum albumin, lysozyme, and hemoglobin. These proteins also bind to both purified DNA and to a nuclear body from dormant spores. Although this binding gives little or no protection to proteins A and B from proteolysis, it does result in elevation of the melting temperature of the DNA by as much as 20degrees.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. M. Carroll and P. Setlow Site-Directed Mutagenesis and Structural Studies Suggest that the Germination Protease, GPR, in Spores of Bacillus Species Is an Atypical Aspartic Acid Protease J. Bacteriol., October 15, 2005; 187(20): 7119 - 7125. [Abstract] [Full Text] [PDF]

				C. S. Hayes and P. Setlow Identification of Protein-Protein Contacts between alpha /beta -Type Small, Acid-soluble Spore Proteins of Bacillus Species Bound to DNA J. Biol. Chem., July 10, 1998; 273(28): 17326 - 17332. [Abstract] [Full Text] [PDF]

				C. S. Hayes, B. Illades-Aguiar, L. Casillas-Martinez, and P. Setlow In Vitro and In Vivo Oxidation of Methionine Residues in Small, Acid-Soluble Spore Proteins from Bacillus Species J. Bacteriol., May 15, 1998; 180(10): 2694 - 2700. [Abstract] [Full Text]

				C. Nessi, A. M. Albertini, M. L. Speranza, and A. Galizzi The outB Gene of Bacillus subtilis Codes for NAD Synthetase J. Biol. Chem., March 17, 1995; 270(11): 6181 - 6185. [Abstract] [Full Text] [PDF]

				C. S. Hayes, Z.-Y. Peng, and P. Setlow Equilibrium and Kinetic Binding Interactions between DNA and a Group of Novel, Nonspecific DNA-binding Proteins from Spores of Bacillus and Clostridium Species J. Biol. Chem., November 3, 2000; 275(45): 35040 - 35050. [Abstract] [Full Text] [PDF]