A disruption‐replacement approach for the targeted integration of foreign genes in <i>Hansenula polymorpha</i>

Agaphonov, Michael O.; Beburov, M. Yu.; Ter‐Avanesyan, Michael D.; Смирнов, В. Н.

doi:10.1002/yea.320111304

Cited by 35 publications

(34 citation statements)

References 25 publications

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“…An elegant disruption-replacement method for targeted single copy integration has recently been described [20]. First, the TRP3 gene of an H. polymorpha leu1.2 strain was disrupted by insertion of the S. cerevisiae LEU2 gene.…”

Section: Expression Vectorsmentioning

confidence: 99%

“…Other heterologous prepro-sequences, which have successfully been used in H. polymorpha are derived from Schwanniomyces occidentalis glucoamylase [5,45], Carcinus maenas hyperglycemic hormone [45], Aspergillus niger glucoamylase [20], Kluyveromyces lactis killer toxin [20], and Kluyveromyces marxianus inulinase [46] (see Table 1). …”

Section: Secretionmentioning

confidence: 99%

“…Proper translation of the presequence could be hampered due to the presence of rare codons for H. polymorpha [20] resulting in a decrease in translation rate or even in a translation block. Adjustments in the coding regions can solve such problems.…”

Section: Secretionmentioning

confidence: 99%

“…Incorrect or incomplete processing of the pre(pro)sequences can also result in reduced secretion efficiency. Examples in H. polymorpha are the secretion of human urinary plasmalogen activator (slow processing of the prosequence) or leech hirudin (incorrect processing resulting in one amino acid extension) [20,45]. These problems are generally related to insufficient recognition of the cleavage site(s) by the processing peptidases.…”

Section: Secretionmentioning

confidence: 99%

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The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Dijk

Faber

Kiel

et al. 2000

Enzyme and Microbial Technology

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Section: Expression Vectorsmentioning

confidence: 99%

Section: Secretionmentioning

confidence: 99%

Section: Secretionmentioning

confidence: 99%

Section: Secretionmentioning

confidence: 99%

See 2 more Smart Citations

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

Dijk

Faber

Kiel

et al. 2000

Enzyme and Microbial Technology

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“…uPA activity assay and zymography. A qualitative test for the ability of yeast transformants to secrete uPA was performed by examination of their capacity to create halos during growth on fibrin-containing medium as described previously (1). Fibrinolytic activity was measured by using a fibrin plate assay (7).…”

Section: Methodsmentioning

confidence: 99%

C-Terminal Truncation of α-COP Affects Functioning of Secretory Organelles and Calcium Homeostasis in Hansenula polymorpha

et al. 2004

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In eukaryotic cells, COPI vesicles retrieve resident proteins to the endoplasmic reticulum and mediate intra-Golgi transport. Here, we studied the Hansenula polymorpha homologue of the Saccharomyces cerevisiae RET1 gene, encoding ␣-COP, a subunit of the COPI protein complex. H. polymorpha ret1 mutants, which expressed truncated ␣-COP lacking more than 300 C-terminal amino acids, manifested an enhanced ability to secrete human urokinase-type plasminogen activator (uPA) and an inability to grow with a shortage of Ca 2؉ ions, whereas a lack of ␣-COP expression was lethal. The ␣-COP defect also caused alteration of intracellular transport of the glycosylphosphatidylinositol-anchored protein Gas1p, secretion of abnormal uPA forms, and reductions in the levels of Pmr1p, a Golgi Ca 2؉ -ATPase. Overexpression of Pmr1p suppressed some ret1 mutant phenotypes, namely, Ca 2؉ dependence and enhanced uPA secretion. The role of COPI-dependent vesicular transport in cellular Ca 2؉ homeostasis is discussed.In eukaryotic cells, secretory proteins synthesized at the endoplasmic reticulum (ER) pass through multiple distinct membrane-bound organelles comprising the secretory pathway. Transport of proteins and lipids between membrane compartments of the early secretory system is mediated by COPIand COPII-coated vesicles that capture cargo, bud from the donor membrane, and then target, dock, and fuse with an appropriate acceptor compartment (40). Both the COPI and COPII protein coat complexes employ a GTP switch mechanism for coating and uncoating. The COPII complex mediates selective protein export from the ER, while COPI-coated vesicles retrieve resident proteins to the ER and mediate intraGolgi transport (8,38).The Golgi apparatus is composed of distinct cisternal regions, namely, the cis, medial, trans-Golgi, and trans-Golginetwork regions (13). Secretory cargo proteins passing through the Golgi apparatus are modified by the unique sets of resident enzymes of different subcompartments. Two alternative models for the origin of the Golgi subcompartments suggest different roles for COPI vesicles in secretory cargo transport and the function of the Golgi apparatus. In the stable-compartments model, anterograde COPI vesicles carry secretory cargo forward and exclude resident Golgi proteins. In the cisternalmaturation model, entire cisternae carry secretory cargo forward, and retrograde COPI vesicles recycle resident Golgi proteins to younger cisternae. Thus, the distinction between the two models centers on the contents of COPI vesicles and the directionality of their transport. However, recent experimental data indicate that intra-Golgi COPI traffic has a bidirectional character (for reviews, see references 23 and 38). Moreover, the dynamics of cisternal progression and vesicular traffic are different in higher eukaryotes versus yeasts. Progression of the tightly stacked Golgi cisternae of animal cells occurs at a significantly lower rate than the traffic of most cargoes through the secretory pathway. COPI vesicles mediating cargo tra...

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Vectors for rapid selection of integrants with different plasmid copy numbers in the yeastHansenula polymorpha DL1

Agaphonov

Trushkina

Sohn

et al. 1999

Yeast

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The authors report about the formation of Al4Cu9 from a thin Cu film evaporated on the five‐fold surface of icosahedral AlPdMn. By heating up to 350°C Al diffuses from the quasicrystal into the Cu film forming well crystalline Al4Cu9 present in 5 domains rotated by 72° with respect to each other and exposed in the (110) surface. The investigation was performed using Low Energy Electron Diffraction, X‐ray Photoelectron Diffraction and X‐ray Photoelectron Spectroscopy giving information about long range order, local structure and chemical composition.

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A disruption‐replacement approach for the targeted integration of foreign genes in Hansenula polymorpha

Cited by 35 publications

References 25 publications

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

The methylotrophic yeast Hansenula polymorpha: a versatile cell factory

C-Terminal Truncation of α-COP Affects Functioning of Secretory Organelles and Calcium Homeostasis in Hansenula polymorpha

Vectors for rapid selection of integrants with different plasmid copy numbers in the yeastHansenula polymorpha DL1

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