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Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation
Author(s) -
Mitchell Clayton,
Morris Paul W.,
Vary James C.
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb00882.x
Subject(s) - bacillus subtilis , biology , triosephosphate isomerase , biochemistry , bacillaceae , amino acid , peptide sequence , bacillales , bacillus (shape) , isomerase , nucleic acid sequence , sequence (biology) , gene , microbiology and biotechnology , bacteria , genetics
Summary Bacillus subtilis cell extracts, prepared at different times during growth, contained several proteins that were apparently guanylylated in vitro with [α‐ 32 P]‐GTP. Four of the proteins were partially purified and the N ‐terminal amino acid sequences (13 to 20 residues) were determined. One sequence had 84% identity to Bacillus stearothermophlius triosephosphate isomerase, two were 100% identical to the predicted sequences of the B. subtilis ptsI and ptsH genes while no identity was found for the fourth sequence. This apparent guanylylation occurred with proteins involved in glucose metabolism, although the significance is unknown.