The GroEL protein is an essential molecular chaperone found in bacteria. Its name is derived from the gene involved in its synthesis, groE, and the size of the protein, which is around 60 kilodaltons. The pronunciation of the word is /ɡroʊˈɛl/ with stress on the second syllable. The "G" is pronounced as the sound of "g" in "go" and "o" is pronounced as in "oh". The "E" is pronounced as in "pet" and "L" as in "ell". The IPA phonetic transcription provides a standardized way of representing the sounds in words for accurate pronunciation.
GroEL protein, also known as chaperonin GroEL, is a highly conserved cellular protein found in prokaryotes, particularly in bacteria. It plays a crucial role as an essential molecular chaperone, which assists in the proper folding of newly synthesized proteins, as well as in refolding and preventing protein aggregation under various cellular stress conditions.
The GroEL protein belongs to the chaperonin family, characterized by a cylindrical structure composed of 14 subunits arranged in two stacked rings. Each subunit has an ATP binding site that undergoes conformational changes upon ATP hydrolysis, facilitating the folding process. The central cavity of GroEL provides an isolated and well-protected environment, allowing proteins to fold without disruptions from external factors.
In its functional form, GroEL typically works in conjunction with another protein called GroES. Upon ATP hydrolysis, the GroES protein binds to one end of GroEL, resulting in a closed lid-like structure called the GroEL-GroES complex. This closure boosts the efficiency of protein folding and prevents aggregation by efficiently encapsulating the substrate protein within the central cavity.
The GroEL protein is involved in various biological processes, including protein homeostasis, cell cycle regulation, and stress response. It has been extensively studied due to its importance in maintaining protein integrity and preventing protein misfolding, which is associated with numerous human diseases, including neurodegenerative disorders and cancer.
The understanding of GroEL protein's structure, function, and interactions provides valuable insights into the fundamental mechanisms of protein folding and opens avenues for developing potential therapeutics for protein misfolding diseases.
The word "GroEL" is an abbreviation derived from the term "green fluorescent protein operon locus". It refers to a family of proteins known as chaperonins that are found in bacteria. The GroEL protein specifically is a heat shock protein that assists in the correct folding of other proteins within the cell. The name "GroEL" is based on the first letter of the scientist's last name who discovered it, GroES (the letter "L" is used to indicate a large protein). Hence, the word "GroEL Protein" is a combination of "Gro" from GroES and "EL" to indicate it is a large protein.