PMID- 12456875
OWN - NLM
STAT- MEDLINE
DCOM- 20030613
LR  - 20190910
IS  - 0269-2139 (Print)
IS  - 0269-2139 (Linking)
VI  - 15
IP  - 9
DP  - 2002 Sep
TI  - Production and characterization of recombinant tachycitin, the Cys-rich 
      chitin-binding protein.
PG  - 763-9
AB  - Tachycitin is an invertebrate chitin-binding protein with an amidated C-terminus, 
      and possesses antimicrobial activity against both fungi and bacteria. The 
      (1)H-NMR-based tertiary structure of tachycitin was recently determined [Suetake 
      et al. (2000) J. Biol. Chem., 275, 17929-17932]. In order to examine the 
      structural and functional features of tachycitin more closely, we performed for 
      the first time, gene expression, refolding, (15)N-NMR-based characterizations, 
      and antimicrobial activity measurements of a recombinant tachycitin (rTcn) that 
      does not have the amide group at the C-terminus. The NMR analysis indicated that 
      rTcn possesses the same structural construction as the native tachycitin. The 
      backbone (15)N relaxation measurements showed that the molecular motional 
      correlation time of rTcn increases as its concentration increases, indicating 
      that tachycitins have a tendency to aggregate with each other. rTcn exhibits 
      antimicrobial activity against fungi but not against bacteria. The cell surface 
      of fungi contains chitin as an essential constituent, but that of bacteria does 
      not. These results suggest that not only the chitin-binding region but also the 
      C-terminal amide group of tachycitin plays a significant role in its 
      antimicrobial properties.
FAU - Suetake, Tetsuya
AU  - Suetake T
AD  - Division of Biological Sciences, Graduate School of Science, Hokkaido University, 
      Sapporo 060-0810, Japan.
FAU - Aizawa, Tomoyasu
AU  - Aizawa T
FAU - Koganesawa, Nozomi
AU  - Koganesawa N
FAU - Osaki, Tsukasa
AU  - Osaki T
FAU - Kobashigawa, Yoshihiro
AU  - Kobashigawa Y
FAU - Demura, Makoto
AU  - Demura M
FAU - Kawabata, Shun-Ichiro
AU  - Kawabata S
FAU - Kawano, Keiichi
AU  - Kawano K
FAU - Tsuda, Sakae
AU  - Tsuda S
FAU - Nitta, Katsutoshi
AU  - Nitta K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Protein Eng
JT  - Protein engineering
JID - 8801484
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Blood Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (tachycitin protein, Tachypleus tridentatus)
RN  - 1398-61-4 (Chitin)
RN  - 9007-49-2 (DNA)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Anti-Bacterial Agents/chemistry/pharmacology
MH  - Base Sequence
MH  - Binding Sites
MH  - Blood Proteins/*chemistry/metabolism/pharmacology
MH  - Carrier Proteins/*chemistry/metabolism/pharmacology
MH  - Chitin/metabolism
MH  - Cysteine/chemistry
MH  - DNA/genetics
MH  - In Vitro Techniques
MH  - Models, Molecular
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Protein Conformation
MH  - Protein Engineering
MH  - Recombinant Proteins/chemistry/metabolism/pharmacology
EDAT- 2002/11/29 04:00
MHDA- 2003/06/14 05:00
CRDT- 2002/11/29 04:00
PHST- 2002/11/29 04:00 [pubmed]
PHST- 2003/06/14 05:00 [medline]
PHST- 2002/11/29 04:00 [entrez]
AID - 10.1093/protein/15.9.763 [doi]
PST - ppublish
SO  - Protein Eng. 2002 Sep;15(9):763-9. doi: 10.1093/protein/15.9.763.