Article
The strongly conserved carboxyl-terminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable.
Molecular microbiology - 1 Jan 1993
McLennan N F, Girshovich A S, Lissin N M, Charters Y, Masters M
Abstract excerpt
The universally distributed heat-shock proteins (HSPs) are divided into classes based on molecular weight and sequence conservation. The members of at least two of these classes, the HSP60s and the HSP70s, have chaperone activity. Most HSP60s and many HSP70s feature a striking motif at or near the carboxyl terminus which consists of a string of repeated glycine and methionine residues. We have altered the groEL...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Chaperonin 60
- Escherichia coli
- Fungal Proteins
- Genes, Bacterial
- Heat-Shock Proteins
- Humans
- Molecular Sequence Data
- Mutagenesis