DNA-dependent RNA polymerase from the extremely halophilic archaebacterium Halococcus morrhuae

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Abstract
Pure and absolutely DNA-dependent RNA polymerase was isolated from the extremely halophilic archaebacterium, H. morrhuae. It is composed of 5 heavy (142,000; 88,000; 73,000; 52,500; and 49,500 Da [dalton]) and 5 small components (13,300; 11,200; 10,800; 10,500; 9900 Da). The peptides of 49,500 and 52,500 Da probably represent 1 component in different modification states. Single-stranded DNa shows the highest template efficiency, although archaebacterial chromosomal DNAs are efficiently transcribed. Rifampicin, streptolydigin and .alpha.-amanitin do not inhibit transcription by this enzyme. Heparin permits elongation, but not initiation of transcription. The activity of H. morrhuae RNA polymerase is strongly stimulated by glycerol and dimethylsulfoxide.