A Study on the Proteins that Interact with Human Nebulin SH3 Domain.
- Author:
Soo Ho CHOI
1
;
Han Suk KO
;
Deok Weon KIM
Author Information
1. Department of Orthopedic Surgery Seoul Paik Hospital, Inje University, Korea. shinabro2000@hanmail.net
- Publication Type:Original Article
- Keywords:
Nebulin;
SH3 domain;
Yeast two-hybrid;
alpha-actinin 2
- MeSH:
Base Sequence;
Clone Cells;
DNA;
Gene Library;
Humans*;
Muscle Contraction;
Muscular Diseases;
Plasmids;
src Homology Domains*;
Yeasts
- From:Journal of Korean Orthopaedic Research Society
2002;5(2):133-139
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
OBJECTIVE: bjective: By identifying the unknown substance responsible for binding with nebulin SH3 domain within the sarcomeric Z-line, we tried to find out Z-line structure which plays an important role on muscle contraction and maintenance of muscle funtion. METHOD: First, the bait plasmid was made by binding the DNA binding domain of Gal4 protein of yeast and the SH3 domain. Second, library plasmid was made by binding activation domain and human skeletal cDNA library. Then, the base sequence of the clone, produced by combining the two proteins expressed by transgenically converted plasmid in yeast, was analyzed. RESULT: We screened out six true positive clones and analyzed the base sequence of the two of six clones. We identified them to be alpha-actinin2. CONCLUSION: We can theorize that Neublin SH3 domain and alpha-actinin2 plays a vital role for the integration of Z-line. Thus, this is an important data in further studying muscle functions, mechanisms, and muscular disease as well.
