The multifunctional or moonlighting protein CD26/DPPIV

2003 ◽  
Vol 82 (2) ◽  
pp. 53-73 ◽  
Author(s):  
Emil Boonacker ◽  
Cornelis J.F. Van Noorden
Keyword(s):  
Moonlighting Protein

Medical and Veterinary Importance of the Moonlighting Functions of Triosephosphate Isomerase

2019 ◽  
Vol 20 (4) ◽  
pp. 304-315 ◽  
Author(s):  
Mónica Rodríguez-Bolaños ◽  
Ruy Perez-Montfort
Keyword(s):  
Cell Cycle ◽  
Immune Response ◽  
Triosephosphate Isomerase ◽  
Dihydroxyacetone Phosphate ◽  
Canonical Function ◽  
Moonlighting Protein ◽  
Veterinary Importance ◽  
Moonlighting Functions

Triosephosphate isomerase is the fifth enzyme in glycolysis and its canonical function is the reversible isomerization of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. Within the last decade multiple other functions, that may not necessarily always involve catalysis, have been described. These include variations in the degree of its expression in many types of cancer and participation in the regulation of the cell cycle. Triosephosphate isomerase may function as an auto-antigen and in the evasion of the immune response, as a factor of virulence of some organisms, and also as an important allergen, mainly in a variety of seafoods. It is an important factor to consider in the cryopreservation of semen and seems to play a major role in some aspects of the development of Alzheimer's disease. It also seems to be responsible for neurodegenerative alterations in a few cases of human triosephosphate isomerase deficiency. Thus, triosephosphate isomerase is an excellent example of a moonlighting protein.

Ceruloplasmin, a moonlighting protein in fish

2018 ◽  
Vol 82 ◽  
pp. 460-468 ◽  
Author(s):  
Sweta Das ◽  
Pramoda Kumar Sahoo
Keyword(s):  
Moonlighting Protein

scholarly journals SpyAD, a Moonlighting Protein of Group A Streptococcus Contributing to Bacterial Division and Host Cell Adhesion

2014 ◽  
Vol 82 (7) ◽  
pp. 2890-2901 ◽  
Author(s):  
Marilena Gallotta ◽  
Giovanni Gancitano ◽  
Giampiero Pietrocola ◽  
Marirosa Mora ◽  
Alfredo Pezzicoli ◽  
...  
Keyword(s):  
Cell Division ◽  
Mammalian Cells ◽  
Group A Streptococcus ◽  
Host Cells ◽  
Knockout Mutant ◽  
Content Type ◽  
Moonlighting Protein ◽  
Group A

ABSTRACTGroup A streptococcus (GAS) is a human pathogen causing a wide repertoire of mild and severe diseases for which no vaccine is yet available. We recently reported the identification of three protein antigens that in combination conferred wide protection against GAS infection in mice. Here we focused our attention on the characterization of one of these three antigens, Spy0269, a highly conserved, surface-exposed, and immunogenic protein of unknown function. Deletion of thespy0269gene in a GAS M1 isolate resulted in very long bacterial chains, which is indicative of an impaired capacity of the knockout mutant to properly divide. Confocal microscopy and immunoprecipitation experiments demonstrated that the protein was mainly localized at the cell septum and could interactin vitrowith the cell division protein FtsZ, leading us to hypothesize that Spy0269 is a member of the GAS divisome machinery. Predicted structural domains and sequence homologies with known streptococcal adhesins suggested that this antigen could also play a role in mediating GAS interaction with host cells. This hypothesis was confirmed by showing that recombinant Spy0269 could bind to mammalian epithelial cellsin vitroand thatLactococcus lactisexpressing Spy0269 on its cell surface could adhere to mammalian cellsin vitroand to mice nasal mucosain vivo. On the basis of these data, we believe that Spy0269 is involved both in bacterial cell division and in adhesion to host cells and we propose to rename this multifunctional moonlighting protein as SpyAD (StreptococcuspyogenesAdhesion andDivision protein).

scholarly journals Inositol Polyphosphate Multikinase (IPMK), a Gene Coding for a Potential Moonlighting Protein, Contributes to Human Female Longevity

Genes ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 125 ◽  
Author(s):  
Francesco De Rango ◽  
Paolina Crocco ◽  
Francesca Iannone ◽  
Adolfo Saiardi ◽  
Giuseppe Passarino ◽  
...  
Keyword(s):  
Genetic Factors ◽  
Inositol Phosphates ◽  
Nutrient Sensing ◽  
Human Longevity ◽  
Cell Physiology ◽  
Inositol Polyphosphate ◽  
Moonlighting Protein ◽  
Key Enzyme ◽  
Female Longevity ◽  
Inositol Polyphosphate Multikinase

Biogerontological research highlighted a complex and dynamic connection between aging, health and longevity, partially determined by genetic factors. Multifunctional proteins with moonlighting features, by integrating different cellular activities in the space and time, may explain part of this complexity. Inositol Polyphosphate Multikinase (IPMK) is a potential moonlighting protein performing multiple unrelated functions. Initially identified as a key enzyme for inositol phosphates synthesis, small messengers regulating many aspects of cell physiology, IPMK is now implicated in a number of metabolic pathways affecting the aging process. IPMK regulates basic transcription, telomere homeostasis, nutrient-sensing, metabolism and oxidative stress. Here, we tested the hypothesis that the genetic variability of IPMK may affect human longevity. Single-SNP (single nuclear polymorphism), haplotype-based association tests as well as survival analysis pointed to the relevance of six out of fourteen genotyped SNPs for female longevity. In particular, haplotype analysis refined the association highlighting two SNPs, rs2790234 and rs6481383, as major contributing variants for longevity in women. Our work, the first to investigate the association between variants of IPMK and longevity, supports IPMK as a novel gender-specific genetic determinant of human longevity, playing a role in the complex network of genetic factors involved in human survival.

scholarly journals Mechanism of action of the moonlighting protein EfTu as a Substance P sensor in Bacillus cereus

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Awa R. N’Diaye ◽  
Valerie Borrel ◽  
Pierre-Jean Racine ◽  
Thomas Clamens ◽  
Segolene Depayras ◽  
...  
Keyword(s):  
Substance P ◽  
Bacillus Cereus ◽  
Mechanism Of Action ◽  
Moonlighting Protein

The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesion

2010 ◽  
Vol 76 (3) ◽  
pp. 605-615 ◽  
Author(s):  
Sarfraz A. Tunio ◽  
Neil J. Oldfield ◽  
Alan Berry ◽  
Dlawer A. A. Ala'Aldeen ◽  
Karl G. Wooldridge ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Neisseria Meningitidis ◽  
Host Cell ◽  
Moonlighting Protein ◽  
Surface Localization

Conformational Characteristics of Rice Hexokinase OsHXK7 as a Moonlighting Protein involved in Sugar Signalling and Metabolism

2017 ◽  
Vol 36 (4) ◽  
pp. 249-256 ◽  
Author(s):  
Li Wang ◽  
Qing Dong ◽  
Qingdong Zhu ◽  
Niwen Tang ◽  
Shenghua Jia ◽  
...  
Keyword(s):  
Moonlighting Protein ◽  
Sugar Signalling

scholarly journals An evolutionary perspective on protein moonlighting

2014 ◽  
Vol 42 (6) ◽  
pp. 1684-1691 ◽  
Author(s):  
Shelley D. Copley
Keyword(s):  
Point Mutations ◽  
Optimal Solution ◽  
Gene Encoding ◽  
Genetic Changes ◽  
Moonlighting Protein ◽  
History Of ◽  
Moonlighting Proteins ◽  
Ultimate Outcome ◽  
Moonlighting Functions ◽  
Population Effects

Moonlighting proteins serve one or more novel functions in addition to their canonical roles. Moonlighting functions arise when an adventitious interaction between a protein and a new partner improves fitness of the organism. Selective pressure for improvement in the new function can result in two alternative outcomes. The gene encoding the newly bifunctional protein may duplicate and diverge so as to encode two proteins, each of which serves only one function. Alternatively, genetic changes that minimize adaptive conflict between the two functions and/or improve control over the time and place at which each function is served can lead to a moonlighting protein. Importantly, genetic changes that enhance a moonlighting function can occur in the gene encoding the moonlighting protein itself, in a gene that affects the structure of its new partner or in a gene encoding a transcription factor that controls expression of either partner. The evolutionary history of each moonlighting protein is complex, depending on the stochastic occurrence of genetic changes such as gene duplication and point mutations, and the effects of those changes on fitness. Population effects, particularly loss of promising individuals due to random genetic drift, also play a role in the emergence of a moonlighting protein. The ultimate outcome is not necessarily the ‘optimal’ solution to the problem of serving two functions, but may be ‘good enough’ so that fitness becomes limited by some other function.

Sign in / Sign up

Export Citation Format

Share Document