[1][2] Studies show that EF-P prevents ribosomes from stalling during the synthesis of proteins containing consecutive prolines.

[7] The elongation phase of translation is promoted by three universal elongation factors, EF-Tu, EF-Ts, and EF-G.[9] EF-P was discovered in 1975 by Glick and Ganoza,[10] as a factor that increased the yield of peptide bond formation between initiator fMet-tRNA(fMet) and a mimic of aa-tRNA, puromycin (Pmn).

The low yield of product formation in absence of EF-P can be described by the loss of peptidyl-tRNA from the stalled ribosome.

To complete its function, EF-P enters paused ribosomes through the E-site and facilitates peptide bond formation through interactions with the P-site tRNA.

[12] Additionally, EF-P has been shown to assist in efficient translation of three or more consecutive proline residues.