Resonance assignments of bacteriophage T4 Y04L protein

  • Kaining Zhang
  • Zhihao Wang
  • Gang Chang
  • Hongliang Wang
  • Yawen Wang
  • Bing LiuEmail author


Phage study draws more attention recently as the bacterial antibiotic resistances become a major threat for global health. Bacteriophage T4 is one of the most studied the phages and the representative of Tevenvirinae subfamily. Since 1950s, T4 phage has been studied more intensively than any other large lytic phages and its biological studies have provided basis for current phage biology as well as other applications. However, among approximately 300 T4 genes, 130 of them still remain uncharacterized. Coded by y04L gene in pin-nrdC intergenic region, Y04L is an example of such proteins whose biological function and mechanism are yet to be addressed. While Pin blocks bacterial Lon protease and thus inhibits bacterial toxin–antitoxin system, NrdC or Glutaredoxin is a specific reducing agent for the phage-induced ribonucleotide reductase. With two interesting neighbouring genes, this 11.9 kDa protein may be functionally related to Pin or NrdC. Here, using solution-state NMR, our near-complete resonance assignment of Y04L provides a basis for future structure determination and further mechanism study.


Escherichia coli Bacteriophage T4 Y04L 11.9 kDa Pin NrdC 


Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.BioBank, First Affiliated Hospital, School of MedicineXi’an Jiaotong UniversityXi’anChina
  2. 2.Instrumental Analysis Center of Xi’an Jiaotong UniversityXi’anChina

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