S. Engeman et al., CARTOGRAPHY OF RIBOSOMAL-PROTEINS OF THE 30S SUBUNIT FROM THE HALOPHILIC HALOARCULA-MARISMORTUI AND COMPLETE SEQUENCE-ANALYSIS OF PROTEIN HS26, European journal of biochemistry, 234(1), 1995, pp. 24-31
By two-dimensional polyacrylamide gel electrophoresis of 30S ribosomal
subunit proteins (S proteins) from Haloarcula marismortui we identifi
ed 27 distinct spots and analyzed all of them by protein sequence anal
ysis. We demonstrated that protein HmaS2 (HS2) is encoded by the open
reading frame orfMSG and has sequence similarities to the S2 ribosomal
protein family. The proteins HmaS5 and HmaS14 were identified as spot
s HS7 and HS21/HS22, respectively. Protein HS4 was characterized by am
ino-terminal sequence analysis. The spot HS25 was recognized as an ind
ividual protein and also characterized by sequence analysis. Furthermo
re, the complete primary sequence of HS26 is reported, showing similar
ity only to eukaryotic ribosomal proteins. The sequence data of a furt
her basic protein shows a high degree of similarity to ribosomal prote
in S12, therefore it was designated HmaS12. Slightly different results
compared to published sequence data were obtained for the proteins HS
12 and HmaS19. The putative 'ribosomal' protein HSH could not be local
ized in the two-dimensional pattern of the total 30S ribosomal subunit
proteins of H. marismortui. Therefore, it seems to be unlikely that t
his protein is a real constituent of the H. marismortui, ribosome.