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Tgl protein: Social motility and st...

Rodriguez-Soto, Jorge Pedro.

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Tgl protein: Social motility and stimulation in Myxococcus xanthus.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Tgl protein: Social motility and stimulation in Myxococcus xanthus./
作者:	Rodriguez-Soto, Jorge Pedro.
面頁冊數:	161 p.
附註:	Adviser: Dale Kaiser.
Contained By:	Dissertation Abstracts International63-01B.
標題:	Biology, Microbiology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3038142
ISBN:	0493519645

Tgl protein: Social motility and stimulation in Myxococcus xanthus.
Rodriguez-Soto, Jorge Pedro.

Tgl protein: Social motility and stimulation in Myxococcus xanthus. - 161 p.

Adviser: Dale Kaiser.

Thesis (Ph.D.)--Stanford University, 2002.

Multiple gene systems are required for the gliding of <italic>Myxococcus xanthus</italic> cells. The social (S) motility system functions in the movement of cells in groups. Mutations in the <italic>tgl</italic> locus result in the absence of S motility and pili, but both S motility and piliation can be restored by mixing <italic>tgl</italic> mutant cells with <italic>tgl</italic><super> +</super> cells. The <italic>tgl</italic> transcription unit was cloned within a 1.7-kb DNA fragment that rescued the <italic>tgl</italic> mutation after ectopic integration at a prophage attachment site. Rescue of the social motility defect by a cloned DNA fragment simultaneously restored the ability to stimulate <italic> tgl</italic> mutants, showing that stimulation required a <italic>tgl</italic><super> +</super> allele. The nucleotide sequence of this fragment revealed two potential protein coding regions, which was confirmed by the construction and expression of hybrid proteins. Complementation tests and transposon insertion revealed that Tgl corresponds to one of these coding regions.

ISBN: 0493519645Subjects--Topical Terms:

1017734
Biology, Microbiology.

Tgl protein: Social motility and stimulation in Myxococcus xanthus.
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245 1 0 $a Tgl protein: Social motility and stimulation in Myxococcus xanthus.
300 $a 161 p.
500 $a Adviser: Dale Kaiser.
500 $a Source: Dissertation Abstracts International, Volume: 63-01, Section: B, page: 0096.
502 $a Thesis (Ph.D.)--Stanford University, 2002.
520 $a Multiple gene systems are required for the gliding of <italic>Myxococcus xanthus</italic> cells. The social (S) motility system functions in the movement of cells in groups. Mutations in the <italic>tgl</italic> locus result in the absence of S motility and pili, but both S motility and piliation can be restored by mixing <italic>tgl</italic> mutant cells with <italic>tgl</italic><super> +</super> cells. The <italic>tgl</italic> transcription unit was cloned within a 1.7-kb DNA fragment that rescued the <italic>tgl</italic> mutation after ectopic integration at a prophage attachment site. Rescue of the social motility defect by a cloned DNA fragment simultaneously restored the ability to stimulate <italic> tgl</italic> mutants, showing that stimulation required a <italic>tgl</italic><super> +</super> allele. The nucleotide sequence of this fragment revealed two potential protein coding regions, which was confirmed by the construction and expression of hybrid proteins. Complementation tests and transposon insertion revealed that Tgl corresponds to one of these coding regions.
520 $a An antiserum that recognized a portion of Tgl detected in wild type <italic> M. xanthus</italic> cells a protein with an apparent molecular weight of 27.5 kDa by sodium dodecylsulfate-polyacrylamide gel electrophoresis. This molecular mass corresponds closely to the molecular mass predicted from the amino acid sequence of Tgl before modification (27,030 Da). This protein antigen is absent from <italic>tgl</italic> mutants generated by transposon insertion within, or deletion of, the chromosomal <italic>tgl</italic> transcription unit. A similar protein is produced in <italic>E. coli</italic> cells that carry a plasmid harboring the <italic>tgl</italic> transcription. Tgl is associated with the membrane of <italic>M. xanthus</italic>, from which it can be solubilized by detergents. Indirect immunofluorescence analysis of whole cells suggests that Tgl is located in the periplasmic space and attached to either the outer or inner membranes, or both. The amino-terminal sequence of Tgl resembles the signal peptides of bacterial lipoproteins that are modified at their amino-termini by fatty acylation. Fatty acids linked to the amino-terminus of Tgl may provide attachment of the protein to the membrane. Tgl contains six tandem repeats of the tetratricopeptide motif which has been shown to mediate protein-protein interactions. Thus, Tgl is likely to interact with other protein(s) in the assembly of the pilus.
590 $a School code: 0212.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
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