Purification and amino acid sequence of two small, acid-soluble proteins from Clostridium bifermentans spores.
Clostridium bifermentans spores contain two major small, acid-soluble, proteins (SASP) termed SASP-alpha and beta. The amino acid sequences of SASP-alpha and beta are almost identical, and are very similar to those of alpha/beta-type SASP from spores of C. perfringens and various Bacillus species. However, the C. bifermentans proteins contain an extra five amino acids in the middle of their sequence. Surprisingly, no gamma-type SASP were found in C. bifermentans or C. perfringens spores, although these are the most prominent SASP in spores of Bacillus species.
Cabrera-Martinez
R M
RM
Department of Biochemistry, University of Connecticut Health Center, Farmington 06032.
Mason
J M
JM
Setlow
B
B
Waites
W M
WM
Setlow
P
P
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification*; D003013:Clostridium / Q000032:analysis*; D008969:Molecular Sequence Data; D012808:Sigma Factor; D013171:Spores, Bacterial / Q000032:analysis; D014157:Transcription Factors
D001426:Bacterial Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus