TY - JOUR
T1 - The Mycobacterium avium-intracellulare complex dnaB locus and protein intein splicing
AU - Yamamoto, K.
AU - Low, B.
AU - Rutherford, S. A.
AU - Rajagopalan, M.
AU - Madiraju, M. V.V.S.
N1 - Funding Information:
We thank Dr. Richard Wallace, Jr. and Ms. Barbara Brown for MAC strains; Drs. S. Ahmad, T. Parish, and Mark Atkinson for interest and helpful comments on the manuscript. This work is supported in part by grants from the National Institutes of Health (AI47045 and AI41406).
PY - 2001
Y1 - 2001
N2 - Intein is a protein sequence mebedded in-frame within a precursor protein and is posttranslationally excised by a self-catalytic protein splicing process. Protein splicing is believed to follow a pathway requiring Cys, Ser, or Thr residues at the intein N-terminus and substitutions other than Cys, Ser, or Thr residues prevent splicing. We show that the dnaB locus in some strains of M. avium-intracellulare complex (MAC) contains intein and that the intein N-terminal amino acid is Ala [Ala-type]. We demonstrate that the M. avium DnaB precursor protein undergoes posttranslational proteolytic processing producing proteins corresponding to the sizes of the DnaB and intein. Further, by Western analysis we detect a protein corresponding to the size of the spliced DnaB protein in MAC cell extracts. Together, these results indicate that the Ala-type MAC DnaB inteins can splice and provide another example that points to an interesting alternative splicing mechanism (Southworth, M. W., Benner, J., and Perler, F. B., EMBO J. 19, 5019-5026, 2000).
AB - Intein is a protein sequence mebedded in-frame within a precursor protein and is posttranslationally excised by a self-catalytic protein splicing process. Protein splicing is believed to follow a pathway requiring Cys, Ser, or Thr residues at the intein N-terminus and substitutions other than Cys, Ser, or Thr residues prevent splicing. We show that the dnaB locus in some strains of M. avium-intracellulare complex (MAC) contains intein and that the intein N-terminal amino acid is Ala [Ala-type]. We demonstrate that the M. avium DnaB precursor protein undergoes posttranslational proteolytic processing producing proteins corresponding to the sizes of the DnaB and intein. Further, by Western analysis we detect a protein corresponding to the size of the spliced DnaB protein in MAC cell extracts. Together, these results indicate that the Ala-type MAC DnaB inteins can splice and provide another example that points to an interesting alternative splicing mechanism (Southworth, M. W., Benner, J., and Perler, F. B., EMBO J. 19, 5019-5026, 2000).
KW - DnaB
KW - Inteins
KW - Mutagenesis
KW - Mycobacteria
KW - Mycobacterium-intracellulare complex
KW - PCR
KW - Protein splicing
UR - https://www.scopus.com/pages/publications/0034810242
UR - https://www.scopus.com/pages/publications/0034810242#tab=citedBy
U2 - 10.1006/bbrc.2000.4202
DO - 10.1006/bbrc.2000.4202
M3 - Article
C2 - 11162608
AN - SCOPUS:0034810242
SN - 0006-291X
VL - 280
SP - 898
EP - 903
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -