Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Rendueles, Paz Suárez

doi:10.1016/0378-1097(88)90239-x

Cited by 20 publications

(17 citation statements)

References 175 publications

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“…This result suggests that the enzyme(s) could be involved in the dimorphic transition of the yeast (data not shown). Seven carboxypeptidases have been described in Saccharomyces cerevisiae (Suárez-Rendueles & Wolf, 1988). We could detect only one carboxypeptidase activity that was located in the soluble fraction.…”

Section: Discussionmentioning

confidence: 67%

The intracellular proteolytic system of Yarrowia lipolytica and characterization of an aminopeptidase

Hernández–Montañez

Araujo-Osorio

Noriega-Reyes

et al. 2007

FEMS Microbiology Letters

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Intracellular proteases of Yarrowia lipolytica have been scarcely studied. These enzymes may play an important role in nitrogen metabolism, posttranslational processing, nutritional stress, dimorphism, etc.; biochemical and genetic control of these enzymes can help in obtaining high-level expression of recombinant proteins in heterologous systems. In this study, we report the presence of three proteases: aminopeptidase yylAPE, carboxypeptidase yylCP and dipeptidyl aminopeptidase yylDAP, measured under several nutritional conditions. Yarrowia lipolytica produced the highest level of intracellular proteolytic enzymes, i.e. yylAPE, yylCP and yylDAP, in media with peptone during stationary growth phase. When soluble extracts were subjected to PAGE, and the three activities were revealed in gels with the corresponding substrates, only one band of activity was detected for each one. The three enzymes were affected by serine protease inhibitors. Chelating agents affected mainly APE activity. The aminopeptidase was purified by selective fractionation with ammonium sulfate and three chromatographic steps (anion exchange, hydrophobic interaction and gel filtration chromatography). The enzyme had a molecular mass of 97 kDa; optimal pH and temperature were 7.0 and 37 degrees C, respectively. The aminopeptidase showed a preference for lysine in the N-position. The K(m) value was 0.86 microM and V(max) value was 990.8 micromoL min(-1) mg(-1) for Lys-pNA.

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Section: Discussionmentioning

confidence: 67%

The intracellular proteolytic system of Yarrowia lipolytica and characterization of an aminopeptidase

Hernández–Montañez

Araujo-Osorio

Noriega-Reyes

et al. 2007

FEMS Microbiology Letters

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“…In the Golgi, the carbohydrate of CPY is modified, resulting in the p2CPY form of 69 kDa. After transport to the vacuole, CPY is matured (mCPY) to a final form of 61 kDa (Rendueles and Wolf, 1988). Figure 7, A and B, shows that the transport of wild-type CPY is not delayed to a significant degree in cells lacking Der1p.…”

Section: Figure 2 (A)mentioning

confidence: 94%

ER-Golgi Traffic Is a Prerequisite for Efficient ER Degradation

Taxis

Vogel

Wolf

2002

MBoC

108

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Protein quality control is an essential function of the endoplasmic reticulum. Misfolded proteins unable to acquire their native conformation are retained in the endoplasmic reticulum, retro-translocated back into the cytosol, and degraded via the ubiquitin-proteasome system. We show that efficient degradation of soluble malfolded proteins in yeast requires a fully competent early secretory pathway. Mutations in proteins essential for ER-Golgi protein traffic severely inhibit ER degradation of the model substrate CPY*. We found ER localization of CPY* in WT cells, but no other specific organelle for ER degradation could be identified by electron microscopy studies. Because CPY* is degraded in COPI coat mutants, only a minor fraction of CPY* or of a proteinaceous factor required for degradation seems to enter the recycling pathway between ER and Golgi. Therefore, we propose that the disorganized structure of the ER and/or the mislocalization of Kar2p, observed in early secretory mutants, is responsible for the reduction in CPY* degradation. Further, we observed that mutations in proteins directly involved in degradation of malfolded proteins (Der1p, Der3/Hrd1p, and Hrd3p) lead to morphological changes of the endoplasmic reticulum and the Golgi, escape of CPY* into the secretory pathway and a slower maturation rate of wild-type CPY.

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“…APs are major N-terminal modifying enzymes which catalyze the hydrolysis of amino acids from the N-terminus of peptides and proteins (Matsui et al, 2006). These enzymes are ubiquitous in nature and their activities have been defined in animals, plants and prokaryotes (McDonald and Barrett, 1986;Rendueles and Wolf, 1988;Walling and Gu, 1996). APs have been well characterized from the germinating and non-germinating seeds of the various plant species such as, barley (Hordeum vulgare) (Sopanen and Mikola, 1975;Ogiwara et al, 2005;Strelec et al, 2009), Japanese apricot (Prunus mume) (Ninomiya et al, 1981), Picea abies (Miiller-Starck and Huttermann, 1981), buckwheat (Fagopyrum esculentum) (Ikeda et al, 1983), jojoba (Simmondsia chinensis) (Johnson and Storey, 1985), Vicia faba (Citharel and Garreau, 1987), Haynaldoticum sardoum (Galleschi and Pellegrini, 1989), kidney bean (Phaseolus vulgaris) (Mikkonen, 1992), mung bean (Vigna radiata) (Yamaoka et al, 1994), Cannabis sativa (Arima et al, 2000), sunflower (Helianthus annuus) (Tishinov et al, 2009), chickpea (Cicer arietinum) (Marinova et al, 2009) and soybean (Glycine max) (Asano et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Changes and induction of aminopeptidase activities in response to pathogen infection during germination of pigeonpea (Cajanas cajan) seeds

Lomate

Hivrale

2011

Journal of Plant Physiology

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Proteinase function in yeast: Biochemical and genetic approaches to a central mechanism of post-translational control in the eukaryote cell

Cited by 20 publications

References 175 publications

The intracellular proteolytic system of Yarrowia lipolytica and characterization of an aminopeptidase

The intracellular proteolytic system of Yarrowia lipolytica and characterization of an aminopeptidase

ER-Golgi Traffic Is a Prerequisite for Efficient ER Degradation

Changes and induction of aminopeptidase activities in response to pathogen infection during germination of pigeonpea (Cajanas cajan) seeds

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