TY - JOUR
T1 - New structural proteins of Halobacterium salinarum gas vesicle revealed by comparative proteomics analysis
AU - Chu, Lichieh Julie
AU - Chen, Mengchieh Claire
AU - Setter, Jocelyn
AU - Tsai, Yihsuan Shannon
AU - Yang, Hanyin
AU - Fang, Xuefeng
AU - Ting, Ying Sonia
AU - Shaffer, Scott A.
AU - Taylor, Gregory K.
AU - Von Haller, Priska D.
AU - Goodlett, David R.
AU - Ng, Wailap Victor
PY - 2011/3/4
Y1 - 2011/3/4
N2 - The Halobacterium salinarum gas vesicle (GV) is an extremely stable intracellular organelle with air trapped inside a proteinaceous membrane. Reported here is a comparative proteomics analysis of GV and GV depleted lysate (GVD) to reveal the membrane structural proteins. Ten proteins encoded by gvp-1 (gvpMLKJIHGFED-1 and gvpACNO-1) and five proteins encoded by gvp-2 (gvpMLKJIHGFED-2 and gvpACNO-2) gene clusters for the biogenesis of spindle- and cylindrical-, respectively, shaped GV were identified by LC-MS/MS. The peptides of GvpA1, I1, J1, A2, and J2 were exclusively identified in purified GV, GvpD1, H1, L1, and F2 only in GVD, and GvpC1, N1, O1, F1, H2, and O2 in both samples. The identification of GvpA1, C1, F1, J1, and A2 in GV is in agreement with their previously known structural function. In addition, the detection of GvpI1, N1, O1, H2, J2, and O2 in GV suggested they are new structural proteins. Among these, the structural role of GvpI1 and N1 in GV was further validated by immuno-detection of protein A-tagged GvpI1 and N1 fusion proteins in purified GV. Thus, LC-MS/MS could reveal at least a half dozen gas vesicle structural proteins in the predominant spindle-shaped GV that may be helpful for studying its biogenesis.
AB - The Halobacterium salinarum gas vesicle (GV) is an extremely stable intracellular organelle with air trapped inside a proteinaceous membrane. Reported here is a comparative proteomics analysis of GV and GV depleted lysate (GVD) to reveal the membrane structural proteins. Ten proteins encoded by gvp-1 (gvpMLKJIHGFED-1 and gvpACNO-1) and five proteins encoded by gvp-2 (gvpMLKJIHGFED-2 and gvpACNO-2) gene clusters for the biogenesis of spindle- and cylindrical-, respectively, shaped GV were identified by LC-MS/MS. The peptides of GvpA1, I1, J1, A2, and J2 were exclusively identified in purified GV, GvpD1, H1, L1, and F2 only in GVD, and GvpC1, N1, O1, F1, H2, and O2 in both samples. The identification of GvpA1, C1, F1, J1, and A2 in GV is in agreement with their previously known structural function. In addition, the detection of GvpI1, N1, O1, H2, J2, and O2 in GV suggested they are new structural proteins. Among these, the structural role of GvpI1 and N1 in GV was further validated by immuno-detection of protein A-tagged GvpI1 and N1 fusion proteins in purified GV. Thus, LC-MS/MS could reveal at least a half dozen gas vesicle structural proteins in the predominant spindle-shaped GV that may be helpful for studying its biogenesis.
KW - Halobacterium salinarum
KW - archaea
KW - gas vesicle
KW - proteomics
KW - structural protein
UR - http://www.scopus.com/inward/record.url?scp=79952408606&partnerID=8YFLogxK
U2 - 10.1021/pr1009383
DO - 10.1021/pr1009383
M3 - Article
C2 - 21158390
AN - SCOPUS:79952408606
SN - 1535-3893
VL - 10
SP - 1170
EP - 1178
JO - Journal of Proteome Research
JF - Journal of Proteome Research
IS - 3
ER -