Alkaline pH responses are widely regulated by phosphorylation mechanisms that profoundly affect transcription. Combining genetic techniques with classical and molecular biochemistry, we have previously characterized in S. cerevisiae the role of several protein phosphatases, such as calcineurin, PP1, Ppz1 or members of the PP2C family in these processes. Our group has been key in understanding the complex signaling network underlying the potent transcriptional remodeling induced by alkaline pH, which involves protein kinases (such as PKA, Snf1\/AMPK, Slt2 or Pho85), protein phosphatases (such as calcineurin) and a multitude of transcription factors. More recently, we have investigated this signaling network in the yeast Komagataella phaffii (Pichia pastoris) due to its biotechnological interest and with the aim of establishing the basis for future alkaline pH-controlled expression platforms.<\/p>\n\n\n\n
Protein levels do not always correspond to the levels of the mRNAs that encode them, indicating the existence of translational control. The importance of this regulation increases in certain conditions, such as cellular stress, which require immediate changes in protein levels. Using ribosome footprinting sequencing and proteomics techniques, we study the effect of alkaline pH on the regulation of translation and develop translation optimization strategies to increase protein production.<\/p>\n\n\n\n
Currently, many proteins of industrial or biomedical interest are produced in yeast through the heterologous expression process. We are developing new platforms for the heterologous expression of proteins in S. cerevisiae and K. phaffii, based on transcriptional elements activated by moderate alkalization. These platforms can improve currently used production processes.<\/p>\n\n\n\n
<\/p>\n","protected":false},"excerpt":{"rendered":"
Alkaline pH stress signaling in yeast Alkaline pH responses are widely regulated by phosphorylation mechanisms that profoundly affect transcription. Combining genetic techniques with classical and molecular biochemistry, we have previously characterized in S. cerevisiae the role of several protein phosphatases, such as calcineurin, PP1, Ppz1 or members of the PP2C family in these processes. Our […]<\/p>\n","protected":false},"author":1831,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-1509","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/pages\/1509","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/users\/1831"}],"replies":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/comments?post=1509"}],"version-history":[{"count":1,"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/pages\/1509\/revisions"}],"predecessor-version":[{"id":1510,"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/pages\/1509\/revisions\/1510"}],"wp:attachment":[{"href":"https:\/\/webs.uab.cat\/gbml\/wp-json\/wp\/v2\/media?parent=1509"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}