Carboxy-Terminal Region Involved in Activity of Escherichia coli TolC

A thioredoxin (BbTrx) was identified from the entomopathogenic fungus Beauveria bassiana . The cloned nucleotide sequence consisted of a 423-bp open reading frame encoding a 141-amino-acid thioredoxin, a 1011-bp 5′ region, and a 419-bp 3′ region. The deduced protein sequence of BbTrx, including a common 95-amino-acid conserved domain and a unique 46-amino-acid carboxy terminal region, was similar (≤38% identity) to that of other thioredoxins and phylogenetically closest to that from Neurospora crassa . In insulin solution containing dithiothreitol at 25 °C, recombinant BbTrx or a truncated form lacking the carboxy terminal region (BbTrxD) exhibited disulfide reduction activity. BbTrxD was more active after pre-incubation at 40–75 °C, and cells expressing BbTrxD showed significantly higher tolerance to thermal stress (51 °C). The BbTrx expression in B. bassiana was greatly elevated when stressed at 40 °C. The results indicate that the new thioredoxin is a potential target for improving the thermotolerance of B. bassiana formulations.

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The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

Molecular and Cellular Biology ◽

10.1128/mcb.14.2.1459-1464.1994 ◽

1994 ◽

Vol 14 (2) ◽

pp. 1459-1464

Author(s):

Y Minami ◽

Y Kimura ◽

H Kawasaki ◽

K Suzuki ◽

I Yahara

Keyword(s):

Amino Acid ◽

Terminal Region ◽

Full Length ◽

Yeast Cells ◽

Amino Acid Residues ◽

Haploid Strain ◽

Carboxy Terminal Region ◽

Carboxy Terminal ◽

Hsp90 Alpha

The majority of mouse HSP90 exists as alpha-alpha and beta-beta homodimers. Truncation of the 15-kDa carboxy-terminal region of mouse HSP90 by digestion with the Ca(2+)-dependent protease m-calpain caused dissociation of the dimer. When expressed in a reticulocyte lysate, the full-length human HSP90 alpha formed a dimeric form. A plasmid harboring human HSP90 alpha cDNA was constructed so that the carboxy-terminal 49 amino acid residues were removed when translated in vitro. This carboxy-terminally truncated human HSP90 alpha was found to exist as a monomer. In contrast, loss of the 118 amino acid residues from the amino terminus of human HSP90 alpha did not affect its in vitro dimerization. Introduction of an expression plasmid harboring the full-length human HSP90 alpha complements the lethality caused by the double mutations of two HSP90-related genes, hsp82 and hsc82, in a haploid strain of Saccharomyces cerevisiae. The carboxy-terminally truncated human HSP90 alpha neither formed dimers in yeast cells nor rescued the lethal double mutant.

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Stability of the Escherichia coli Division Inhibitor Protein MinC Requires Determinants in the Carboxy-Terminal Region of the Protein

Journal of Bacteriology ◽

10.1128/jb.180.1.175-177.1998 ◽

1998 ◽

Vol 180 (1) ◽

pp. 175-177 ◽

Cited By ~ 8

Author(s):

Mita Sen ◽

Lawrence I. Rothfield

Keyword(s):

Escherichia Coli ◽

Terminal Region ◽

Lon Protease ◽

Inhibitor Protein ◽

Loss Of Function ◽

Cellular Concentration ◽

Carboxy Terminal Region ◽

The Stability ◽

Carboxy Terminal

ABSTRACT Certain mutations in the C-terminal region of the Escherichia coli division inhibitor protein MinC cause loss of function of the division inhibitor by making MinC more sensitive to degradation by Lon protease, implying a possible role for the C-terminal region in regulating the stability and cellular concentration of MinC.

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The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo.

Molecular and Cellular Biology ◽

10.1128/mcb.14.2.1459 ◽

1994 ◽

Vol 14 (2) ◽

pp. 1459-1464 ◽

Cited By ~ 115

Author(s):

Y Minami ◽

Y Kimura ◽

H Kawasaki ◽

K Suzuki ◽

I Yahara

Keyword(s):

Amino Acid ◽

Terminal Region ◽

Full Length ◽

Yeast Cells ◽

Amino Acid Residues ◽

Haploid Strain ◽

Carboxy Terminal Region ◽

Carboxy Terminal ◽

Hsp90 Alpha

The majority of mouse HSP90 exists as alpha-alpha and beta-beta homodimers. Truncation of the 15-kDa carboxy-terminal region of mouse HSP90 by digestion with the Ca(2+)-dependent protease m-calpain caused dissociation of the dimer. When expressed in a reticulocyte lysate, the full-length human HSP90 alpha formed a dimeric form. A plasmid harboring human HSP90 alpha cDNA was constructed so that the carboxy-terminal 49 amino acid residues were removed when translated in vitro. This carboxy-terminally truncated human HSP90 alpha was found to exist as a monomer. In contrast, loss of the 118 amino acid residues from the amino terminus of human HSP90 alpha did not affect its in vitro dimerization. Introduction of an expression plasmid harboring the full-length human HSP90 alpha complements the lethality caused by the double mutations of two HSP90-related genes, hsp82 and hsc82, in a haploid strain of Saccharomyces cerevisiae. The carboxy-terminally truncated human HSP90 alpha neither formed dimers in yeast cells nor rescued the lethal double mutant.

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Carboxy-Terminal Region of Escherichia coli SecA ATPase Is Important to Promote Its Protein Translocation Activity in Vivo

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1994.1617 ◽

1994 ◽

Vol 200 (3) ◽

pp. 1477-1483 ◽

Cited By ~ 23

Author(s):

T. Rajapandi ◽

D. Oliver

Keyword(s):

Escherichia Coli ◽

Protein Translocation ◽

Terminal Region ◽

Carboxy Terminal Region ◽

Carboxy Terminal

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Functional Analysis of Potential Carboxy-Terminal Cleavage Sites of Tick-Borne Encephalitis Virus Capsid Protein

Journal of Virology ◽

10.1128/jvi.02116-07 ◽

2007 ◽

Vol 82 (5) ◽

pp. 2218-2229 ◽

Cited By ~ 10

Author(s):

Sabrina Schrauf ◽

Petra Schlick ◽

Tim Skern ◽

Christian W. Mandl

Keyword(s):

Amino Acid ◽

Capsid Protein ◽

Protein C ◽

Terminal Region ◽

Encephalitis Virus ◽

Viral Protease ◽

Tick Borne Encephalitis ◽

Carboxy Terminal Region ◽

Tick Borne Encephalitis Virus ◽

Carboxy Terminal

ABSTRACT The mature capsid protein C of flaviviruses is generated through the proteolytic cleavage of the precursor polyprotein by the viral NS2B/3 protease. This cleavage is a prerequisite for the subsequent processing of the viral surface protein prM, and the concerted progression of these events plays a key role in the process of the assembly of infectious virions. Protein C of tick-borne encephalitis virus (TBEV) contains two amino acid sequence motifs within the carboxy-terminal region that match the canonical NS2B/3 recognition site. Site-specific mutagenesis in the context of the full-length TBEV genome was used to investigate the in vivo cleavage specificity of the viral protease in this functionally important domain. The results indicate that the downstream site is necessary and sufficient for efficient cleavage and virion assembly; in contrast, the upstream site is dispensable and placed in a structural context that renders it largely inaccessible to the viral protease. Mutants with impaired C-prM cleavage generally exhibited a significantly increased cytotoxicity. In spite of the clear preference of the protease for only one of the two naturally occurring motifs, the enzyme was unexpectedly tolerant to both the presence of a noncanonical threonine residue at position P2 and the position of cleavage relative to the adjacent internal prM signal sequence. The insertion of three amino acid residues downstream of the cleavage site did not change the viral phenotype. Thus, this study further illuminates the specificity of the TBEV protease and reveals that the carboxy-terminal region of protein C has a remarkable functional flexibility in its role in the assembly of infectious virions.

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