Different DNA-binding proteins in the primary and secondary forms of Xenorhabdus luminescens.
Basic, heat-stable proteins binding to double-stranded DNA (HASP) were isolated from the primary and secondary forms of Xenorhabdus luminescens and their composition compared. Two of the proteins with low molecular weight are present in both the primary and secondary forms, whereas two others are present only in the latter. The described protein fractions may be involved in the regulation of transitions between the two forms of X. luminescens.
Popowska
M
M
Department of Bacterial Physiology, University of Warsaw, Poland.
Dziechniarz
K
K
Paterczyk
B
B
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D004755:Enterobacteriaceae / Q000378:metabolism*; D008970:Molecular Weight
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins