Secretion of the Streptomyces tyrosinase is mediated through its trans-activator protein, MelC1.

Leu, Wei-Ming; Chen, Lingyun; Liaw, Li-Ling; Lee, Yan-Hwa Wu

doi:10.1016/s0021-9258(19)88672-6

Cited by 52 publications

(23 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was also surprising to find that the alteration introduced in the residues preceding the signal peptidase cleavage site in the YA33SM mutant caused a moderate export defect in Npr (Figures 4 and 5), whereas a similar substitution at the corresponding region in MelC1 signal peptide yielded no detectable effects on export [8]. This contrast might reflect their respective secondary structures at the processing site.…”

Section: Discussionmentioning

confidence: 97%

“…It is also important to know whether the signal peptide sequences in these two streptomycete proteins, MelC1 and Npr, have the same features in regard to their export function. Previously we reported the effects of mutations in the MelC1 signal peptide on its secretion and trans-activation functions [8].…”

Section: Figure 1 Proposed Model For Maturation and Secretion Of Nprmentioning

confidence: 99%

“…In comparison, however, the secretory mechanisms of Gram-positive bacteria such as Bacillus or Streptomyces have received insufficient characterization. Few signal peptide sequence mutants in these two genera have been reported [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

“…systems for the study of Streptomyces secretory proteins. MelC1 has an N-terminal signal peptide sequence and acts as the molecular chaperone for apotyrosinase (MelC2) ; it has a dual role in secretion and trans-activation of apo-tyrosinase [8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi

Chang¹,

Su²,

Lee³

1997

Biochemical Journal

View full text Add to dashboard Cite

The neutral metalloprotease (Npr) of Streptomyces cacaoi is synthesized as a prepro-Npr precursor form consisting of a secretory signal peptide, a propeptide and the mature metalloprotease. The maturation of Npr occurs extracellularly via an autoproteolytic processing of the secreted pro-Npr. The integrity of the propeptide is essential for the formation of mature active Npr but not for its secretion [Chang, Chang and Lee (1994) J. Biol. Chem. 269, 3548-3554]. In this study we investigated whether the secretion and maturation of Npr require the integrity of its signal peptide region and mature protease domain. Five signal peptide mutants were generated, including the substitution mutations at the positively charged region (mutant IR6LE), the central hydrophobic region (mutants GI19EL and G19N), the boundary of the hydrophobic core-cleavage region (mutant P30L) and at the residues adjacent to the signal peptidase cleavage site (mutant YA33SM). All these lesions delayed the export of Npr to the growth medium and also resulted in a 2-10-fold decrease in Npr export. The most severe effect was noted in mutants GI19EL and P30L. When these signal peptide mutations were fused separately with the propeptide lacking the Npr mature domain, the secretory defect on the propeptide was also observed, and this impairment was again more severely expressed in mutants GI19EL and P30L. Thus the Npr signal peptide seems to have more constraints on the hydrophobic core region and at the proline residue within the boundary of the hydrophobic core-cleavage site. Deletion mutations within the C-terminal mature protease domain that left its active site intact still blocked the proteolytic processing of mutant precursor forms of pro-Npr, although their secretions were unaffected. These results, together with our previous findings, strongly suggest that the signal peptide of Npr plays a pivotal role in the secretion of both Npr and the propeptide, but not in the maturation of Npr. On the contrary, the integrity of mature domain and propeptide is not critical for secretion of the Npr derivative but is essential for the formation of a functional Npr. Therefore the secretion and maturation of Npr are dependent on the integrity of the signal peptide, propeptide and mature protease domains, and the roles of these domains in this regard are functionally distinct.

show abstract

Section: Discussionmentioning

confidence: 97%

Section: Figure 1 Proposed Model For Maturation and Secretion Of Nprmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi

Chang¹,

Su²,

Lee³

1997

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Also, MelC1 is hypothesized to facilitate the secretion of MelC2 in wild-type S. antibioticus since it contains a characteristic Tat (twin-arginine translocation) signal peptide sequence (24,25). MelC1 is postulated to carry MelC2 during secretion (26). After the completion of copper insertion and secretion, MelC1 dissociates from MelC2, and the copper-incorporated MelC2 holoenzyme exhibits tyrosinase activity (27).…”

mentioning

confidence: 99%

Tat-Dependent Heterologous Secretion of Recombinant Tyrosinase by Pseudomonas fluorescens Is Aided by a Translationally Fused Caddie Protein

Ryu

Byun

Park

et al. 2019

Appl Environ Microbiol

View full text Add to dashboard Cite

Tyrosinase is a monooxygenase that catalyzes both the hydroxylation of p-hydroxyphenyl moieties to o-catechols and the oxidation of o-catechols to o-quinones. Apart from its critical functionality in melanogenesis and the synthesis of various neurotransmitters, this enzyme is also used in a variety of biotechnological applications, most notably mediating covalent cross-linking between polymers containing p-hydroxyphenyl groups, forming a hydrogel. Tyrosinases from the genus Streptomyces are usually secreted as a complex with their caddie protein. In this study, we report an increased secretion efficiency observed when the Streptomyces antibioticus tyrosinase gene melC2 was introduced into Pseudomonas fluorescens along with its caddie protein gene melC1, which has the DNA sequence for the Tat (twin-arginine translocation) signal. IMPORTANCE We observed that the S. antibioticus extracellular tyrosinase secretion level was even higher in its nonnatural translationally conjugated fusion protein form than in the natural complex of two separated polypeptides. The results of this study demonstrate that tyrosinase-expressing P. fluorescens can be a stable source of bacterial tyrosinase through exploiting the secretory machinery of P. fluorescens.

show abstract

Ascidian tyrosinase gene: Its unique structure and expression in the developing brain

et al. 1997

View full text Add to dashboard Cite

Tadpole larvae of ascidians have two sensory pigment cells in the brain. One is the otolith cell that functions as a gravity receptor, the other pigment cell is part of a primitive photosensory structure termed the ocellus. These sensory cells, like vertebrate pigment cells, contain membrane‐bounded melanin granules and are considered to reflect a crucial position in the evolutionary process of this cell type. To investigate the molecular changes accompanying the evolution of pigment cells, we have isolated from Halocynthia roretzi a gene encoding tyrosinase, a key enzyme in melanin biosynthesis. The cDNA has an open reading frame (ORF) of 596 amino acids, which is 36–39% identical in amino acid sequence to vertebrate tyrosinases. In addition, the sequence analysis of both cDNA and genomic clones reveals an unusual organization of the tyrosinase gene, an extraordinary 3′ untranslated region of the transcripts with significant homology to the coding sequence, and a single short intron in the sequence encoding a cytoplasmic domain. Expression of the gene is detected first in two pigment precursor cells positioned in the neural plate of early neurulae, and later in two melanin‐containing pigment cells within the brain of late tailbud embryos. Its expression pattern correlates well with the appearance of tyrosinase enzyme activity in the developing brain. These results provide the first description of pigment cell differentiation at the molecular level in the ascidian embryo, and also will contribute to a better understanding of the evolution of chordate pigment cells. Dev. Dyn. 208:363–374, 1997. © 1997 Wiley‐Liss, Inc.

show abstract

Secretion of the Streptomyces tyrosinase is mediated through its trans-activator protein, MelC1.

Cited by 52 publications

References 33 publications

Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi

Roles of the signal peptide and mature domains in the secretion and maturation of the neutral metalloprotease from Streptomyces cacaoi

Tat-Dependent Heterologous Secretion of Recombinant Tyrosinase by Pseudomonas fluorescens Is Aided by a Translationally Fused Caddie Protein

Ascidian tyrosinase gene: Its unique structure and expression in the developing brain

Contact Info

Product

Resources

About