Two new human DNAJ-like proteins

DETAILED DESCRIPTION What is claimed is: 1.
An isolated and purified polynucleotide sequence encoding the amino acid sequence of SEQ ID NO:1.
2.
A composition comprising the polynucleotide sequence of claim 1.
3.
A polynucleotide sequence which is fully complementary to the polynucleotide sequence of claim 2.
4.
An isolated and purified polynucleotide sequence comprising SEQ ID NO:2.
5.
A composition comprising the polynucleotide sequence of claim 4.
6.
A polynucleotide sequence which is fully complementary to the polynucleotide sequence of claim 4.
7.
An expression vector containing the polynucleotide sequence of claim 1.
8.
A host cell containing the vector of claim 7.
9.
A method for producing a polypeptide comprising the amino acid sequence of SEQ ID NO:1, the method comprising the steps of: a) culturing the host cell of claim 8 under conditions suitable for the expression of the polypeptide; and b) recovering the polypeptide from the host cell culture.




Description:
FIELD OF THE INVENTION This invention relates to nucleic acid and amino acid sequences of two new human DnaJ-like proteins and to the use of these sequences in the diagnosis, prevention, and treatment of cancer and inflammatory and immune disorders.
BACKGROUND OF THE INVENTION Induction of heat shock proteins (Hsps), a class of molecular chaperones, is a physiological and biochemical response to abrupt increases in temperature or exposure to a variety of other metabolic insults including heavy metals, amino acid analogs, toxins, and oxidative stress.
This response occurs in all prokaryotic and eukaryotic cells and is characterized by repression of normal protein synthesis and initiation of transcription of Hsp-encoding genes.
Under normal or nonstressed conditions, constitutively expressed Hsps facilitate proper protein folding and maturation, promote protein translocation across membranes, and regulate hormone receptor and protein kinase activity (Hightower, L.
E.
, et al.
(1991) Cell, 66: 191-197).
During cellular stress, Hsps form a complex with proteins that misfold or unfold, either "rescuing" these proteins from irreversible damage or increasing their susceptibility to proteolytic attack