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Upon translocation, the N-MTS is cleaved by the mitochondrial processing peptidase (MPP).
In the mitochondria matrix, the N-terminal signal is usually cleaved off by the Mitochondrial Processing Peptidase MPP [ 9, 10], while the corresponding chloroplast targeting N-terminal signals are processed by an analogous protease in the chloroplast stroma [ 10].
It is nuclearly encoded and produced in the cytoplasm as a 210 amino acid protein that is then imported into the mitochondrion where it is matured into its final form (residues 81-210) by the mitochondrial processing peptidase (MPP) (Schmucker et al., 2008).
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The proteins are: mitochondrial translocase of the outer membrane 40 (TOM40), chaperonin 60 (cpn60) and the α-subunit of the mitochondrial processing peptidase (α-MPP).
One major difference between yeast and plants is the location of the mitochondrial processing peptidase (MPP).
It is often the case that in these circumstances the MTS is cleaved upon entry into the mitochondrion by a mitochondrial processing peptidase (MPP) [30].
protein tags), could arguably represent the best conjugation platform for targeted delivery of molecules into mitochondria because MTS has a well-proven role in guiding proteins into mitochondria and also because MTS can be specifically and precisely processed by mitochondrial processing proteinases (MPP) to release the delivered molecular cargo in the mitochondria.
PINK1 is unique among all protein kinases since it possesses a N-terminal targeting motif that localizes it to the mitochondria where it undergoes sequential cleavage by mitochondrial processing protease and the rhomboid protease PARL (presenilin-associated rhomboid-like protein, mitochondrial) followed by rapid degradation by the N-end rule pathway [ 17].
5 Previous studies suggested that specific mutations (G130V, I154F) might be processed differently by mitochondrial processing peptidase, thus affecting their ability to enter mitochondria.
Most MLS are cleaved by a mitochondrial processing peptidase (MPP) that recognizes a special sequence comprising a positive arginine residue at position −2 and/or −10 from the cleavage site [23], [24].
However, in the liver, GABA-T is further cleaved to a smaller isoform by a second proteolytic step catalyzed by a mitochondrial processing peptidase [ 6].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com