Literature DB >> 23420616

Haloferax mediterranei GlnK proteins are post-translationally modified by uridylylation.

Laia Pedro-Roig1, Mónica Camacho, María José Bonete.   

Abstract

In this work we report for the first time a post-translational modification of PII homologues from the Archaea Domain. Haloferax mediterranei is the first haloarchaea whose PII proteins have been studied, it possesses two of them (GlnK1 and GlnK2 ), both encoded adjacent to a gene for the ammonia transporter Amt. An approach based on 2DE, anti-GlnK immunoblot and peptide mass fingerprint (MALDI-TOF-MS) of the reactive spots showed that GlnK proteins in H. mediterranei are post-translationally uridylylated. A third spot with lower pI suggests the existence of a non-descript post-translational modification in this protein family.
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2013        PMID: 23420616     DOI: 10.1002/pmic.201200465

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  2 in total

1.  Nitrogen regulation of protein-protein interactions and transcript levels of GlnK PII regulator and AmtB ammonium transporter homologs in Archaea.

Authors:  Laia Pedro-Roig; Christian Lange; María José Bonete; Jörg Soppa; Julie Maupin-Furlow
Journal:  Microbiologyopen       Date:  2013-08-28       Impact factor: 3.139

Review 2.  The PII-NAGK-PipX-NtcA Regulatory Axis of Cyanobacteria: A Tale of Changing Partners, Allosteric Effectors and Non-covalent Interactions.

Authors:  Alicia Forcada-Nadal; José Luis Llácer; Asunción Contreras; Clara Marco-Marín; Vicente Rubio
Journal:  Front Mol Biosci       Date:  2018-11-13
  2 in total

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