Mutant of Escherichia coli with thermosensitive protein in the process of cellular division.
نویسندگان
چکیده
A new thermosensitive mutant of Escherichia coli deficient in cell division was isolated by means of membrane filtration after nitrosoguanidine mutagenesis. The mutant cells grow normally at 30 C but stop dividing immediately after shift to 42 C, resulting in multinucleated filaments lacking septa. The number of colony-forming units does not decrease for at least 6 hr at 42 C. The maximum length of the filaments is 10 to 16 times that of normal cells. Addition of a high concentration of NaCl fails to stimulate cell division at 42 C. The filaments formed at 42 C divide abruptly 30 min after shift to 30 C, and synchronous increase of cell number is shown for 3 hr. The macromolecular synthesis of protein and nucleic acids at 42 C is normal on the whole. The cell division shown after the shift from 42 to 30 C is observed in the absence of thymine, but not in the presence of chloramphenicol or in a medium deficient in amino acids. However, the filament can divide to some extent in the presence of chloramphenicol if some protein synthesis is allowed to proceed at 30 C before the addition of the antibiotic. The elongated cells divide at 42 C provided that they are exposed to 30 C before being shifted to high temperature.
منابع مشابه
Soluble Expression and Purification of Q59L Mutant L-asparaginase in the Presence of Chaperones in SHuffle™ T7 strain
Background and Aims: Q59L mutant of L-asparaginase enzyme from Escherichia coli (E. coli) has been introduced with lower side effects. This version of the enzyme might have potential applications in the treatment of leukemia patients. We utilized SHuffle T7 strain of E. coli, to produce the mutant enzyme in the presence of chaperone molecules. Materials and Methods: Q59LAsp gene was cloned in...
متن کاملFuzzy Hybrid least-Squares Regression Approach to Estimating the amount of Extra Cellular Recombinant Protein A from Escherichia coli BL21
Introduction: Immune Protein A is a component with a vast spectrum of biochemical, biological and medical usages. The coding gene of this protein was extracted from Staphylococcus aureus and was cloned and expressed in Escherichia coli bacteria. Suitable statistical methods are utilized to optimize expression conditions for evaluating experiment accuracy , guarantee the accuracy of subsequent ...
متن کاملConstruction of Hybrid Gene of Hepatitis B Surface Antigen Carrying Heat-Stable Enterotoxin of Escherichia coli and Its Expression in Mammalian Cell Line
Hepatitis B surface antigen is the first genetically engineered vaccine licensed for human use. Various strategies have been proposed to obtain a vaccine that would bypass the need for injection. In this study, a non-toxic portion of heat-stable enterotoxin of Escherichia coli that is capable of adhering to epithelial cells was inserted at amino acid position 112 of hepatitis surface antigen. T...
متن کاملConstruction of an iss deleted mutant strain from a native avian pathogenic Escherichia coli O78: K80 and in vitro serum resistance evaluation of mutant
BACKGROUND: Colibacillosis, caused by different serotypes of avian pathogenic Escherichia coli (APEC), is one of the important diseases in poultry industry. The isolate O78 is the most prevalent serotype of APEC in Iran. One of the APEC virulence factors, increased serum survival (iss) gene, is related to serum resistance. The usual form of colibacillosis in avian is extraintestinal, and serum ...
متن کاملGenetical and physiological studies on a thermosensitive mutant of Escherichia coli defective in cell division.
A new temperature-sensitive mutant of E. coli, defective in cell division, was isolated after selection for tolerance to colicin E2. The mutant strain, ASHI24, growing in either minimal or complex medium, commences filament formation immediately upon shift to high temperature. High densities of bacteria or the presence of 0-44 M-sucrose prevents filament formation at 42 degrees C and division c...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Journal of bacteriology
دوره 112 2 شماره
صفحات -
تاریخ انتشار 1972