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Cysteine-independent polymerization of metallothioneins in solutions and in crystals

Published online by Cambridge University Press:  10 February 2001

TINGJUN HOU
Affiliation:
College of Chemistry and Molecular Engineering, Peking University, Beijing 10087, People's Republic of China
YU AN
Affiliation:
College of Life Sciences, Peking University, Beijing 100871, People's Republic of China
BINGGEN RU
Affiliation:
College of Life Sciences, Peking University, Beijing 100871, People's Republic of China
RUCHANG BI
Affiliation:
Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China
XIAOJIE XU
Affiliation:
College of Chemistry and Molecular Engineering, Peking University, Beijing 10087, People's Republic of China
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Abstract

Polymerization of metallothioneins is one of the usually encountered puzzles during the research process of metallothioneins' structure and function. Our work focuses on the cysteine independently occurred polymerization from metallothioneins monomers in different milieus, while it leaves out the aggregation caused by the oxidation of cysteine, because the latter circumstance is the result of purification lapsus. After the purification of metallothioneins monomers, a dynamic light-scattering technique is used to detect the polymerized states of rabbit liver metallothionein I and II in different buffers, which is the first systematical detection of polymerized states of metallothioneins in solutions. The effects of different compositions of each buffer are discussed in details. Steric complementarity, hydrophobic, and electrostatic interaction characteristics are studied, following the modeling of monomers and relevant polymers of rat metallothionein II, rabbit liver metallothionein I and II. These theoretical calculations are the first complete computer simulations on different factors affecting metallothioneins' polymerization. A molecular recognition mechanism of metallothioneins' polymerization in solutions is proposed on the bases of experimental results and theoretical calculations. Preliminary X-ray studies of two crystal forms of rabbit liver metallothionein II are compared with the crystal structure of rat metallothionein II, and the polymerized states in crystal packing are discussed with the knowledge of polymerization of metallothioneins in solutions. The hypothesis, which is consistent with theoretical calculations and experimental results, is expected to construct a connection between the biochemical characteristics and physiological functions of metallothioneins, and this research may give some enlightenment to the topics of protein polymerizations.

Type
Research Article
Information
Protein Science , Volume 9 , Issue 12 , December 2000 , pp. 2302 - 2312
Copyright
© 2000 The Protein Society

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