Literature DB >> 28097094

Corrigendum.

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Abstract

[This corrects the article DOI: 10.1002/2211-5463.12131.].

Entities:  

Year:  2016        PMID: 28097094      PMCID: PMC5221429          DOI: 10.1002/2211-5463.12165

Source DB:  PubMed          Journal:  FEBS Open Bio        ISSN: 2211-5463            Impact factor:   2.693


In the paper by Matsumoto et al. 1, some text in the Results and Discussion sections appeared incorrectly: Sec signal should have read Tat signal. The correct text appears below:

Results

Based on SignalP prediction, the N‐terminal sequence of the active form of the enzyme starts at Thr28 of the deduced aa sequence, indicating that the preceding 27‐aa residues represent a Tat signal peptide sequence containing a twin‐arginine translocation (Tat) pathway motif (S/T‐R‐R‐X‐Hyd‐Hyd) that is required for secretion (Fig. 2).

Discussion

The signal peptide of LyPls‐PLD had a typical Tat signal sequence, suggesting that it should be secreted via the secretory pathway (Tat‐system secretion) [22]. In addition, reference [22] should be: 22 Lee PA, Tullman‐Ercek D and Georgiou G (2006) The bacterial twin‐arginine translocation pathway. Ann Rev Microbiol 60, 373–395. http://doi.org/10.1146/annurev.micro.60.080805.142212.
  1 in total

1.  Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D from Thermocrispum sp.

Authors:  Yusaku Matsumoto; Nana Kashiwabara; Takayuki Oyama; Kazutaka Murayama; Hideyuki Matsumoto; Shin-Ich Sakasegawa; Daisuke Sugimori
Journal:  FEBS Open Bio       Date:  2016-10-17       Impact factor: 2.693

  1 in total

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