Yeast cytochrome c is a sequence-specific DNA-binding protein

Bhatnagar, Anshu; Raghavendra, Pralhada Rao; Kranthi, Balla Venkata; Rangarajan, Pundi N.

doi:10.1016/j.bbrc.2004.07.044

Cited by 7 publications

(4 citation statements)

References 18 publications

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“…Two cytochromes c are found also in the fruit fly Drosophila melanogaster , in the African malaria mosquito Anopheles gambiae , in the Caenorhabditis worms, in the transparent sea squirt Ciona intestinalis , in the parasites of the Plasmodium genus, and in the fungi of the Saccharomyces genus, where the expression of cytochromes c is regulated by partial oxygen pressure . It has also been proposed that yeast cytochrome c is a sequence-specific DNA-binding protein and might have a regulatory role in the nucleus . The plants Arabidopsis thaliana and Oryza sativa (rice) each contain three cytochromes c , one of which is of the so-called c 6 type (see also section 5.1.11).…”

Section: Eukaryotamentioning

confidence: 99%

“…31 It has also been proposed that yeast cytochrome c is a sequence-specific DNA-binding protein and might have a regulatory role in the nucleus. 32 The plants Arabidopsis thaliana and Oryza satiVa (rice) each contain three cytochromes c, one of which is of the so-called c 6 type (see also section 5.1.11). Plant cytochromes c 6 are targeted to the thylakoid lumen of chloroplasts 33 but do not function alongside plastocyanin in photosynthetic electron flow, and a regulatory or accessory role was proposed 34 for these proteins.…”

Section: Eukaryotamentioning

confidence: 99%

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Cytochromec: Occurrence and Functions

2005

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Section: Eukaryotamentioning

confidence: 99%

Section: Eukaryotamentioning

confidence: 99%

Cytochromec: Occurrence and Functions

2005

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“…Cyt c isolated from rabbit heart was not able to bind to this sequence. Mutations within the UAS which were described to abolish the ability to activate transcription in vivo also abolished cyt c binding in vitro [141]. Besides its role in respiration by transferring electrons from complex III to complex IV of the respiratory chain, cyt c is also involved in apoptotic pathways after its release from mitochondria (e.g.…”

Section: Reviewmentioning

confidence: 99%

Untitled

2006

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Methylotrophic yeasts such as Candida boidinii, Hansenula polymorpha, Pichia methanolica and Pichia pastoris are an emerging group of eukaryotic hosts for recombinant protein production with an ever increasing number of applications during the last 30 years. Their applications are linked to the use of strong methanol-inducible promoters derived from genes of the methanol utilisation pathway. These promoters are tightly regulated, highly repressed in presence of non-limiting concentrations of glucose in the medium and strongly induced if methanol is used as carbon source. Several factors involved in this tight control and their regulatory effects have been described so far. This review summarises available data about the regulation of promoters from methanol utilisation pathway genes. Furthermore, the role of cis and trans acting factors (e.g. transcription factors, glucose processing enzymes) in the expression of methanol utilisation pathway genes is reviewed both in the context of the native cell environment as well as in heterologous hosts.

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“…Recently, Bhatnagar et al (2004) showed that methanol induced the release of cytochrome c from mitochondoria to cytosol in P. pastoris , and cytochrome c had a binding activity to upstream activation sequence (UAS) of the AOX2 promoter. Cytochrome c is known as an apoptosis signal and in S. cerevisiae CYC1–GFP is a fusion protein localized in the nucleus (Huh et al , 2003).…”

Section: Discussionmentioning

confidence: 99%

Peroxisomal metabolism is regulated by an oxygen‐recognition system through organelle crosstalk between the mitochondria and peroxisomes

Fujimura

Nakagawa

Ito

et al. 2007

Yeast

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In the present study using Pichia methanolica, it was found that expressions of methanol-metabolic enzymes were strictly regulated by the presence of oxygen, and that induction of alcohol oxidase (AOD) isozymes was completely dependent on oxygen concentrations. A proportion of AOD-isozyme species responded to oxygen conditions, e.g. in a low oxygen condition, Mod1p was dominant, but with an increase in the oxygen concentration, the ratio of Mod2p increased. The K m value of Mod1p for oxygen was ca. one-seventh lower than that of Mod2p (0.47 and 3.51 mM, respectively). This shows that Mod1p is suitable at low oxygen concentrations and Mod2p at high oxygen concentrations. Also, zymogram changes for AOD isozymes were observed by inhibition of respiratory chain activity. These indicated that P. methanolica has the ability to recognize oxygen conditions and the respiratory chain should participate in the sensor for available oxygen. These facts indicate that there is organelle crosstalk between mitochondria and peroxisomes through nucleus gene regulation in order to control the consumption balance of available oxygen between the mitochondrial respiratory chain and peroxisomal AODs.

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Yeast cytochrome c is a sequence-specific DNA-binding protein

Cited by 7 publications

References 18 publications

Cytochromec: Occurrence and Functions

Cytochromec: Occurrence and Functions

Untitled

Peroxisomal metabolism is regulated by an oxygen‐recognition system through organelle crosstalk between the mitochondria and peroxisomes

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