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Light micrograph of a moss's leaf cells at 400X magnification. The following outline is provided as an overview of and topical guide to cell biology: . Cell biology – A branch of biology that includes study of cells regarding their physiological properties, structure, and function; the organelles they contain; interactions with their environment; and their life cycle, division, and death.
The cellular components of prokaryotes are not enclosed in membranes within the cytoplasm, like eukaryotic organelles. Bacteria have microcompartments, quasi-organelles enclosed in protein shells such as encapsulin protein cages, [4] [5] while both bacteria and some archaea have gas vesicles. [6] Prokaryotes have simple cell skeletons.
The bactofilin protein, BacM, is required for proper cell shape maintenance and cell wall integrity. M. xanthus cells lacking BacM have a deformed morphology characterized by a bent cell body, and bacM mutants have decreased resistance to antibiotics targeting the bacterial cell wall.
Mpa delivers the substrate protein to the proteasome for degradation by coupling of ATP hydrolysis. The discovery of Pup indicates that like eukaryotes, bacteria may use a small-protein modifier to control protein stability. The Pup gene encodes a 64–amino acid protein with a molecular size of about 6.9 kDa. [3]
DNA polymerase I obtained from E. coli is used extensively for molecular biology research. However, the 5'→3' exonuclease activity makes it unsuitable for many applications. This undesirable enzymatic activity can be simply removed from the holoenzyme to leave a useful molecule called the Klenow fragment, widely used in molecular biology.
50S, roughly equivalent to the 60S ribosomal subunit in eukaryotic cells, is the larger subunit of the 70S ribosome of prokaryotes. The 50S subunit is primarily composed of proteins but also contains single-stranded RNA known as ribosomal RNA (rRNA). rRNA forms secondary and tertiary structures to maintain the structure and carry out the catalytic functions of the ribosome.
It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. [2] [3] [4] It is found in eukaryotic mitochondria as TUFM. [5]
Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.