An introduction to protein moonlighting

2014 ◽  
Vol 42 (6) ◽  
pp. 1679-1683 ◽  
Author(s):  
Constance J. Jeffery
Keyword(s):  
Transcription Factors ◽  
Protein Sequence ◽  
Polypeptide Chain ◽  
Biochemical Pathways ◽  
Single Polypeptide Chain ◽  
Potential Benefits ◽  
Moonlighting Proteins ◽  
Structure Databases ◽  
Single Polypeptide ◽  
And Function

Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain performs multiple physiologically relevant biochemical or biophysical functions. Almost 300 proteins have been found to moonlight. The known examples of moonlighting proteins include diverse types of proteins, including receptors, enzymes, transcription factors, adhesins and scaffolds, and different combinations of functions are observed. Moonlighting proteins are expressed throughout the evolutionary tree and function in many different biochemical pathways. Some moonlighting proteins can perform both functions simultaneously, but for others, the protein's function changes in response to changes in the environment. The diverse examples of moonlighting proteins already identified, and the potential benefits moonlighting proteins might provide to the organism, such as through coordinating cellular activities, suggest that many more moonlighting proteins are likely to be found. Continuing studies of the structures and functions of moonlighting proteins will aid in predicting the functions of proteins identified through genome sequencing projects, in interpreting results from proteomics experiments, in understanding how different biochemical pathways interact in systems biology, in annotating protein sequence and structure databases, in studies of protein evolution and in the design of proteins with novel functions.

Multitalented actors inside and outside the cell: recent discoveries add to the number of moonlighting proteins

2019 ◽  
Vol 47 (6) ◽  
pp. 1941-1948 ◽  
Author(s):  
Constance J. Jeffery
Keyword(s):  
Molecular Mechanisms ◽  
Food Crops ◽  
Bacterial Strains ◽  
Cellular Processes ◽  
Biochemical Pathways ◽  
The Past ◽  
Single Polypeptide Chain ◽  
New Antibiotics ◽  
Moonlighting Proteins ◽  
Single Polypeptide

During the past few decades, it's become clear that many enzymes evolved not only to act as specific, finely tuned and carefully regulated catalysts, but also to perform a second, completely different function in the cell. In general, these moonlighting proteins have a single polypeptide chain that performs two or more distinct and physiologically relevant biochemical or biophysical functions. This mini-review describes examples of moonlighting proteins that have been found within the past few years, including some that play key roles in human and animal diseases and in the regulation of biochemical pathways in food crops. Several belong to two of the most common subclasses of moonlighting proteins: trigger enzymes and intracellular/surface moonlighting proteins, but a few represent less often observed combinations of functions. These examples also help illustrate some of the current methods used for identifying proteins with multiple functions. In general, a greater understanding about the functions and molecular mechanisms of moonlighting proteins, their roles in the regulation of cellular processes, and their involvement in health and disease could aid in many areas including developing new antibiotics, predicting the functions of the millions of proteins being identified through genome sequencing projects, designing novel proteins, using biological circuitry analysis to construct bacterial strains that are better producers of materials for industrial use, and developing methods to tweak biochemical pathways for increasing yields of food crops.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres

scholarly journals Hepatic microsomal epoxide hydrase. Chemical evidence for a single polypeptide chain.

1979 ◽  
Vol 254 (14) ◽  
pp. 6240-6243 ◽  
Author(s):  
G C DuBois ◽  
E Appella ◽  
R Armstrong ◽  
W Levin ◽  
A Y Lu ◽  
...  
Keyword(s):  
Polypeptide Chain ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Chemical Evidence

scholarly journals Identification of Igh-C-linked determinants on suppressor T cell hybrids and factors specific for L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT).

1985 ◽  
Vol 162 (3) ◽  
pp. 1044-1059 ◽  
Author(s):  
C M Sorensen ◽  
R J Hayashi ◽  
C W Pierce
Keyword(s):  
T Cells ◽  
T Cell ◽  
Polypeptide Chain ◽  
Spleen Cells ◽  
Suppressor T Cell ◽  
Cell Hybrids ◽  
Single Polypeptide Chain ◽  
Functional Classes ◽  
Single Polypeptide ◽  
Ig Allotype

Hyperimmunization of BALB/c mice with concanavalin A-stimulated blasts from the Ig allotype-congenic strain, C.B20, results in the production of antibodies reactive with T cells in an allotype-restricted manner. Spleen cells from these hyperimmune BALB/c mice were used to generate a panel of hybridomas that secrete monoclonal antibodies, reactive, in an allotype-restricted manner, exclusively with T cells subpopulations, and in particular, reactive with suppressor T cell hybridomas and their secreted soluble factors. Two functional classes of antibodies were identified: those that react with single polypeptide-chain suppressor T cell factors (TsF1) and the suppressor T cell hybridomas that produce such factors, and those that react with two polypeptide-chain suppressor T cell factors (TsF2) and their corresponding suppressor T cell hybridomas. These two classes of antibody were used to isolate molecules from the membranes of the respective suppressor T cell hybrids that are functionally and structurally related to the secreted suppressor T cell factors, suggesting a receptor function for these molecules.

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

scholarly journals The purification and some properties of rusticyanin, a blue copper protein involved in iron(II) oxidation from Thiobacillus ferro-oxidans

1978 ◽  
Vol 174 (2) ◽  
pp. 497-502 ◽  
Author(s):  
J C Cox ◽  
D H Boxer
Keyword(s):  
Polypeptide Chain ◽  
Iron Oxidation ◽  
Exchange Chromatography ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Optical Absorbance ◽  
Single Polypeptide Chain ◽  
Arginine Residues ◽  
Single Polypeptide

The ‘blue’ copper-containing protein rusticyanin was purified to homogeneity from cells of the chemolithotrophic bacterium Thiobacillus ferro-oxidans by (NH4)SO4 fractionation and ion-exchange chromatography. The protein, which is stable at low pH, consists of a single polypeptide chain of mol. wt. 16500 and possesses 0.79 (+/- 0.28)g-atom of Cu/mol. The protein, which does not contain arginine residues, has optical absorbance maxima at 287, 450, 597 and 750 nm and is generally similar to azurin. The isolated protein is reduced directly by Fe2+ with a 1:1 stoicheiometry to Cu. On reduction by Fe2+ the absorption peaks at 450, 597 and 750 nm are abolished, with the appearance of a new absorption band at 320 nm. The results obtained are consistent with rusticyanin being the initial acceptor of electrons from Fe2+ during respiratory iron oxidation.

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