Article Figures & Data
Figures
- Fig. 1.
DNA sequence analysis of malA. Glycosyl hydrolase and ATP/GTP binding motifs are indicated by double and single underlining, respectively. Putative promoter and termination sequences are in boldface. The start of transcription is indicated as +1.
- Fig. 2.
Northern blot analysis of the malA region. (A) Schematic diagram of the malA region. Numbers indicate G+C mole percent compositions. (B, C, and D) Northern blots of themalA region. (B) Lane 1, probe P1; lane 2, probe P2. (C) Lane 1, probe P2; lane 2, probe P3; lane 3, probe P4. (D) Riboprobes. Lane 1, probe P5; lane 2, probe P6.
- Fig. 3.
Primer extension analysis of malA. Lanes 1 to 4, DNA sequencing reactions (T, C, G, and A, respectively); lane 5, primer extension product.
- Fig. 4.
Gel shift analysis of the malA promoter region. Lane 1, probe (malA p-L); lane 2, probe and 5 μg of cell extract; lane 3, probe, extract, and unlabeled probe; lane 4, probe, extract, and unlabeled competitor (malA p-S); lane 5, probe, extract, and unlabeled pUC19 DNA. A and B indicate the positions of retarded complexes. At the bottom schematic diagrams ofmalA fragments used as probe and competitor are shown.
- Fig. 5.
Distribution of malA determined by Southern blot analysis. The probe comprised bp 714 to 1445 of malA. (A) EcoRV digests. (B) HindIII digests. Lanes: 1, S. shibatae DNA; 2, S. acidocaldarius DNA; 3, S. solfataricus 98/2 DNA; 4, S. solfataricus P2 DNA.
- Fig. 6.
Phylogenetic analysis of α-glucosidase and sucrase isomaltase sequences. A neighbor-joining distance tree is shown. Distances are indicated by the bar in the lower left corner, which represents 10 substitutions per 100 residues. Percent occurrence is given for nodes with values of >30%. Lower values are not shown or are indicated by a dash. Left-hand values are measures of distance; right-hand values are measures of parsimony. GenBank accession numbers are shown to the right of the names of the source organisms.
- Fig. 7.
pH optima for maltose and glycogen hydrolysis. (A) Maltose hydrolysis; (B) glycogen hydrolysis. Buffers were as follows: pH 2.0 to 5.0, 100 mM sodium acetate (closed circles); pH 3.5 to 9.0, 100 mM sodium phosphate (open circles).
Tables
- Table 1.
Generation times and α-glucosidase activities ofSulfolobus species during growth on different sole carbon and energy sources
Organism Generation time (h) on: Sp acta (μmol ofp-nitro- phenol/min/mg) on: Glucose Maltose Starch Glucose Maltose Starch S. solfataricus98/2 8 8 10 130 ± 3 221 ± 9 230 ± 26 S. shibatae 12 9 14 29 ± 2 181 ± 21 228 ± 35 S. acidocaldarius 23 NGb 12 <0.1 NDc 12 ± 2
