Cloning of the C-terminal cytoplasmic fragment of the tar protein and effects of the fragment on chemotaxis of Escherichia coli

A gene encoding only the C-terminal portion of the receptor-transducer protein Tar of Escherichia coli was constructed. The gene product was detected and localized in the cytoplasmic fraction of the cell by immunoblotting with anti-Tar antibodies. The C-terminal fragments from wild-type and mutant tar genes were characterized in vivo. The C-terminal fragment generated from tar-526, a mutation that results in a dominant "tumble" phenotype, was found to be deamidated and methylated by the CheB and CheR proteins, respectively. The C-terminal fragment derived from a wild-type gene was poorly deamidated, and the C-terminal fragment derived from tar-529, a dominant mutant with a "smooth swimming" phenotype, was not apparently modified. Cells carrying the C-terminal fragment with the tar-526 mutation as the sole receptor-transducer protein showed a high frequency of tumbling and chemotaxis responses to changes in intracellular pH. These results suggest that the cytoplasmic C-terminal fragment of Tar retains some of the functions of the whole protein in vivo

Acquisition of Maltose Chemotaxis in Salmonella typhimurium by the Introduction of the Escherichia coli Chemosensory Transducer Gene

Escherichia coli and Salmonella typhimurium are closely related species. However, E. coli cells show maltose chemotaxis but S. typhimurium cells do not. When an E. coli chemotransducer gene (tar_E), the product of which is required for both aspartate and maltose chemotaxis, was introduced by using a plasmid vector into S. typhimurium cells with a defect in the corresponding gene (tar_S), the transformant cells acquired the ability for both aspartate and maltose chemotaxis. In contrast, when the tar_s gene was introduced into tar_E-deficient E. coli cells, the transformant cells acquired aspartate chemotaxis but not maltose chemotaxis. These results indicate that the absense of maltose chemotaxis in S. typhimurium is a consequence of the properties of the tar_s gene product

Proper motion and apparent contraction in J0650+6001

We present a multi-epoch and multi-frequency VLBI study of the compact radio source J0650+6001. In VLBI images the source is resolved into three components. The central component shows a flat spectrum, suggesting the presence of the core, while the two outer regions, with a steeper spectral index, display a highly asymmetric flux density. The time baseline of the observations considered to derive the source expansion covers about 15 years. During this time interval, the distance between the two outer components has increased by 0.28+/-0.13 mas, that corresponds to an apparent separation velocity of 0.39c+/-0.18c and a kinematic age of 360+/-170 years. On the other hand, a multi-epoch monitoring of the separation between the central and the southern components points out an apparent contraction of about 0.29+/-0.02 mas, corresponding to an apparent contraction velocity of 0.37c+/-0.02c. Assuming that the radio structure is intrinsically symmetric, the high flux density ratio between the outer components can be explained in terms of Doppler beaming effects where the mildly relativistic jets are separating with an intrinsic velocity of 0.43c+/-0.04c at an angle between 12 and 28 degrees to the line of sight. In this context, the apparent contraction may be interpreted as a knot in the jet that is moving towards the southern component with an intrinsic velocity of 0.66c+/-0.03c, and its flux density is boosted by a Doppler factor of 2.0.Comment: 7 pages, 5 pages. Accepted for publication in MNRA