Although subcellular mRNA trafficking has been demonstrated as a mechanism to control protein distribution, it is generally believed that most protein localization occurs subsequent to translation.
Most protein localization systems recognize conserved motifs encoded at either the N- or C-terminus of their substrates.
In most cases protein localization is not exclusive to a particular sub-cellular compartment or structure.
In T. thermophila studies, the most commonly used protein localization tag is the enhanced green fluorescent protein (EGFP), which is more stable and emits brighter fluorescence than wild-type GFP (WT-GFP).
The most commonly used protein localization tag in T. thermophila is a S65T mutant version of EGFP [ 3, 6, 10, 11, 26- 32], which has recently been codon adapted for knockout studies in T. thermophila as a C-terminal protein localization tag [ 6].
This supports the idea that most protein production is site-specific and suggests that mRNA localization has a prominent role in forming localized cellular machinery.
Most protein molecules are transported by energy-dependent transport mechanisms initiated by nuclear localization signals (NLS).
Most protein mimics of DNA have strikingly hydrophobic cores that likely stabilize the protein fold despite substantial charge localization and a relatively small internal volume enforced by the restrictions from DNA size.
From Table 4, we were able to explore the meaning of each rule, and by checking the rules we discovered the 10 most important features affecting protein localization included MIT1, GLYC, MAYOUNG, GGSI, POX1, SIGNALP, PLMNEW1, TMS1, KNOCKOUT, NUC2.
To date, LocSigDB is the most comprehensive compendium of protein localization signals for eight distinct subcellular locations.
