Molecular genetics of ØX174 Lysis /
(PPlases), suggesting that S]yD is a member of the FKBP
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1996.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | (PPlases), suggesting that S]yD is a member of the FKBP ability to lyse the host cells carrying slvd null alleles abundance. The sequence of the N-terminal 150 residues of and the H. influenza slyd gene is fully capable of because multiple loci were involved. slyd is able to because of a catastrophic defect in the developing septum. been found, suggesting that the pos4b changes are the only changes sufficient to overcome the slyD- block. Host mutants complement the growth defect caused by slyd] in E. coli C, complementing E. coli slyd in terms of lysis function. A context of the phage or from a plasmid vector, to lyse the direct selection of lysis proficient E plasmids in a slyd- E, has been repeatedly isolated and no other E mutant has eliminate the ability of the E gene, expressed in its normal eliminating the lysis ability of the E pos4b mutant were entirely imbedded in an alternate reading frame of another essential gene. E has a hydrophobic N-terminus with one group of slyd missense and deletion mutants that block the host. The pos4b mutant, comprising two missense changes in host. slyd encodes a 196 aa cytoplasmic protein of moderate isolated, but did not map to a chromosomal locus, probably lytic function of the OX174 E gene but retain S]yD protein mechanism of action is unknown. Phage-infected cells lyse of the primary sequence is rich in basic and hydrophilic only viral cistron required for lysis of the host, is protein family. In this study, E mutants restoring the provide important tools for further genetic and biochemical putative membrane-spanning domain, whereas the C-terminal 2/3 Recessive knockout mutations in single host locus slyD residues. E has been localized to the inner membrane but its S]yD is homologous to FK506binding proteins (FKBP), an stability were isolated, characterized, and mapped to a structure modeled on a mammalian FKBP. These slyd mutants studies on the unique molecular mechanism of lysis by OX174. The 91 codon E gene of the small ssDNA phage OX 1 74, the ubiquitous family of peptidyl prolyl cis-trans isomerases were isolated by different mutagenesis methods followed by |
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| Item Description: | "Major subject: Biochemistry". In title, symbols are used. Vita. |
| Physical Description: | xi, 114 leaves : illustrations ; 28 cm. Also available online. Issued also on microfiche from Lange Micrographics. |
| Bibliography: | Includes bibliographical references. |