scholarly journals Enzymes, pseudoenzymes, and moonlighting proteins: diversity of function in protein superfamilies

FEBS Journal ◽  
2020 ◽  
Vol 287 (19) ◽  
pp. 4141-4149 ◽  
Author(s):  
Constance J. Jeffery
Keyword(s):  
Protein Superfamilies ◽  
Moonlighting Proteins

scholarly journals Moonlighting in Bacillus subtilis: The Small Proteins SR1P and SR7P Regulate the Moonlighting Activity of Glyceraldehyde 3-Phosphate Dehydrogenase A (GapA) and Enolase in RNA Degradation

2021 ◽  
Vol 9 (5) ◽  
pp. 1046
Author(s):  
Inam Ul Haq ◽  
Sabine Brantl
Keyword(s):  
Bacillus Subtilis ◽  
Antisense Rna ◽  
Rna Binding ◽  
Rna Degradation ◽  
Metabolic Enzyme ◽  
Dual Function ◽  
Small Proteins ◽  
Moonlighting Proteins ◽  
Rnase Y

Moonlighting proteins are proteins with more than one function. During the past 25 years, they have been found to be rather widespread in bacteria. In Bacillus subtilis, moonlighting has been disclosed to occur via DNA, protein or RNA binding or protein phosphorylation. In addition, two metabolic enzymes, enolase and phosphofructokinase, were localized in the degradosome-like network (DLN) where they were thought to be scaffolding components. The DLN comprises the major endoribonuclease RNase Y, 3′-5′ exoribonuclease PnpA, endo/5′-3′ exoribonucleases J1/J2 and helicase CshA. We have ascertained that the metabolic enzyme GapA is an additional component of the DLN. In addition, we identified two small proteins that bind scaffolding components of the degradosome: SR1P encoded by the dual-function sRNA SR1 binds GapA, promotes the GapA-RNase J1 interaction and increases the RNase J1 activity. SR7P encoded by the dual-function antisense RNA SR7 binds to enolase thereby enhancing the enzymatic activity of enolase bound RNase Y. We discuss the role of small proteins in modulating the activity of two moonlighting proteins.

scholarly journals Comparison of DNA binding across protein superfamilies

2009 ◽  
Vol 78 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Bruno Contreras-Moreira ◽  
Javier Sancho ◽  
Vladimir Espinosa Angarica
Keyword(s):  
Dna Binding ◽  
Protein Superfamilies

Evolution of moonlighting proteins: insight from yeasts

2014 ◽  
Vol 42 (6) ◽  
pp. 1715-1719 ◽  
Author(s):  
Carlos Gancedo ◽  
Carmen-Lisset Flores ◽  
Juana M. Gancedo
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Present Article ◽  
Catabolite Repression ◽  
Kluyveromyces Lactis ◽  
Approaches To Studying ◽  
Moonlighting Proteins ◽  
Experimental Approaches ◽  
Gal Genes

The present article addresses the possibilities offered by yeasts to study the problem of the evolution of moonlighting proteins. It focuses on data available on hexokinase from Saccharomyces cerevisiae that moonlights in catabolite repression and on galactokinase from Kluyveromyces lactis that moonlights controlling the induction of the GAL genes. Possible experimental approaches to studying the evolution of moonlighting hexose kinases are suggested.

scholarly journals On the Origin of Protein Superfamilies and Superfolds

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Abram Magner ◽  
Wojciech Szpankowski ◽  
Daisuke Kihara
Keyword(s):  
Protein Superfamilies

scholarly journals Moonlighting in Mitosis: Analysis of the Mitotic Functions of Transcription and Splicing Factors

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1554 ◽  
Author(s):  
Maria Patrizia Somma ◽  
Evgeniya N. Andreyeva ◽  
Gera A. Pavlova ◽  
Claudia Pellacani ◽  
Elisabetta Bucciarelli ◽  
...  
Keyword(s):  
Evolutionary Process ◽  
Splicing Factors ◽  
Insufficient Data ◽  
Primary Role ◽  
Interphase Nuclei ◽  
Protein Databases ◽  
Moonlighting Proteins ◽  
Bona Fide ◽  
Cellular Compartments ◽  
Moonlighting Functions

Moonlighting proteins can perform one or more additional functions besides their primary role. It has been posited that a protein can acquire a moonlighting function through a gradual evolutionary process, which is favored when the primary and secondary functions are exerted in different cellular compartments. Transcription factors (TFs) and splicing factors (SFs) control processes that occur in interphase nuclei and are strongly reduced during cell division, and are therefore in a favorable situation to evolve moonlighting mitotic functions. However, recently published moonlighting protein databases, which comprise almost 400 proteins, do not include TFs and SFs with secondary mitotic functions. We searched the literature and found several TFs and SFs with bona fide moonlighting mitotic functions, namely they localize to specific mitotic structure(s), interact with proteins enriched in the same structure(s), and are required for proper morphology and functioning of the structure(s). In addition, we describe TFs and SFs that localize to mitotic structures but cannot be classified as moonlighting proteins due to insufficient data on their biochemical interactions and mitotic roles. Nevertheless, we hypothesize that most TFs and SFs with specific mitotic localizations have either minor or redundant moonlighting functions, or are evolving towards the acquisition of these functions.

Sign in / Sign up

Export Citation Format

Share Document