Secretion and degradation of mutant leucine‐specific binding protein molecules containing C‐terminal deletions

Landick, Robert; Duncan, James R.; Copeland, Bruce R.; Nazos, Penelope M.; Oxender, Dale L.

doi:10.1002/jcb.240240404

Cited by 5 publications

(3 citation statements)

References 27 publications

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“…Proteolytic events in this compartment of the cell include processing of signal sequences for exported proteins and turnover of abnormal proteins (4,11,14). Much less evidence is available for turnover of native functional proteins.…”

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confidence: 99%

Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

1989

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The degP gene, required for proteolysis in the cell envelope of Escherichia coli, maps at approximately 3.5 min on the chromosome. Null mutations in degP result in temperature-sensitive growth. In certain genetic backgrounds, expression of abnormal periplasmic or inner membrane proteins (protein fusions or proteins with internal deletions) enhances the temperature-sensitive phenotype. Such growth defects were used as a selection for cloning the degP gene into Mud4042 and pACYC184 plasmid vectors, and a restriction map was determined. Analysis of deletion and insertion mutations on one of these plasmids showed that the degP gene is approximately 1.5 kilobases in size. The plasmid-encoded DegP protein had an apparent molecular weight of 50,000, as determined by maxicell analysis. Protein fusions between DegP and alkaline phosphatase had high alkaline phosphatase enzymatic activity, indicating that DegP is a periplasmic or membrane protein.

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confidence: 99%

Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

1989

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“…In this model, a major role of the membrane potential is suggested for the proper membrane orientation of the proposed helix hairpin formed by the signal sequence and the first segment of the mature portion of the BP [ 16,171, Recent work on the secretion of the BPs has been directed toward identifying the sequences required to achieve secretion. To this end, mutants of LS-BP carrying various deletions or sequence alterations have been constructed [17]. It was found that these altered binding proteins were processed and secreted normally.…”

Section: Secretion Of the Bps Into The Periplasmmentioning

confidence: 99%

The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function

Antonucci

Landick

Oxender

1985

J of Cellular Biochemistry

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The genes encoding the leucine binding proteins in E coli have been cloned and their DNA sequences have been determined. One of the binding proteins (LIV-BP) binds leucine, isoleucine, valine, threonine, and alanine, whereas the other (LS-BP) binds only the D- and L-isomers of leucine. These proteins bind their solutes as they enter the periplasm, then interact with three membrane components, livH, livG, and livM, to achieve the translocation of the solute across the bacterial cell membrane. Another feature of the binding proteins is that they must be secreted into the periplasmic space where they carry out their function. The amino acid sequence of the two binding proteins is 80% homologous, indicating that they are the products of an ancestral gene duplication. Because of these characteristics of the leucine binding proteins, we are using them as models for studying the relationships between protein structure and function.

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“….The first group includes pauses that occur about 8-12 nucleotides downstream from a 'hairpin' stem-loop structure in the transcript. The best-studied example is in the frp attenuator region, rrpt [7]. Recent evidence suggests that DNA sequences downstream of the trpL pause site also determine pause half-life [10,12].…”

Section: Introductionmentioning

confidence: 99%

Transcript hairpin structures are not required for RNA polymerase pausing in the gene encoding the E. coli RNase P RNA, M1 RNA

Ramamoorthy

Schmidt

1991

FEBS Letters

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Strong pauses at nucleotides + I 18 and + I21 relative to the transcriptional star1 occur during in vitro transcription of the E. co/i npB gene encoding the catalytic MI RNA subunit of Ribonucleasc P. These pauses arc immediately downstream of 2 phylogcne~ically conserved stem-loop structures in the RNA. In the prescnl work, single-base changes which disrupted Watson-Crick base-pairing in the hairpins wcrc introduced into r@. Transcription studies in vhro with these modified tcmplaics revealed that none of the nucleotide changes predicted to increase or decrease the stability of the first hairpin significamly affected the ptWX hair-lives. A mutation which disruplcd the second hairpin increased the pause half-IiFc a-fold. The data suggest that 111c upstream stem and loop structures in the transcript arc not involved in the pausing event.RNA structure; Transcription

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Secretion and degradation of mutant leucine‐specific binding protein molecules containing C‐terminal deletions

Cited by 5 publications

References 27 publications

Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function

Transcript hairpin structures are not required for RNA polymerase pausing in the gene encoding the E. coli RNase P RNA, M1 RNA

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