Drosophila Heat Shock Protein
HSP70
Heat shock proteins are produced in response to heat and other physiological stresses. Their main job is to act as molecular chaperones to assist other proteins in folding or refolding into their functional configuration. There are five different HSPs in Drosophila, and there are two copies of the HSP70 gene located close together on the third chromosome. HSP70 has two main domains: the first two-thirds of the sequences is an ATPase, and the last third is the peptide binding domain. The ATPase domain is similar to that of the muscle protein actin. The peptide binding domain holds an extended section of 5-7 hydrophobic amino acids between alpha-helical and beta sheet subdomains. The energy from ATP, released by the ATPase, helps to refold the "chaperoned" protein. As in the muscle protein actin, the binding of ATP makes the peptide binding site available.
Heat Shock Protein 70
Drosophila SequenceATP-binding domain
( ) = Alpha Helix
[ ] = Beta Sheet
{ } = Turns
Peptide-binding domainMPA[IGID]LGTT[YSCVGVYQ]{HG}[KVEI]IAN{DQ}GNRT
[TP]SY[VAF]TDSE[RLI]{G}
(DPAKN)
QVAM{NPRN}[TV]FD
(AKRL)
{IG}RKYDD
(PKIAEDM)
{KH}WPF[KVVSD]{GG}[KPKIGVEY]{KG}[ESKRFA]
(PEEISSMVLTKMKETAEAYL)
GESIT[DAV ITV]P{AY}FN
(DSQRQATKDAGHI)
{AG}L[NVLRIIN]
(EPTAAALA)
{YGLD}KNLKG[ERNVLIFDL]GGGT
(FDVSILTIDE)
{G}SLFEVR[STAGD]{THLG}
(GEDFDNRLVTHLA EEFKRK)
YKKDL{RS}N
(PRALRRLRTAAERAKRT)
[LSS]ST[EATIEI]{DAL}F{EG}QD[ FYTKVS]
(RARFEELCADLFRN){T}(LQPVEKALND)
{AK}MDKGQIH[DIVLV]GGSTR I
(PKVQSLLQEF)
{FHG}KNLNLSIN{PDE}
(AVAYGAAVQAAIL){SG}DQSGKIQDVLLVDVAPLSLGIETAGGVMTKLIERNCRIPCKQTKTFSTYA
DNQPGVSIQVYEGERAMTKDNNALGTFDLSGIPPAPRGVPQIEVTFDLDA
NGILNVSAKEMSTGKAKNITIKNDKGRLSQAEIDRMVNEAEKYADEDEKH
RQRITSRNALESYVFNVKQAVEQAPAGKLDEADKNSVLDKCNDTIRWLDS
NTTAEKEEFDHKLEELTRHCSPIMTKMHQQGAGAGAGGPGANCGQQAGGF
GGYSGPTVEEVD
Notes on the Music:
This piece is a straightforward single read-through of the HSP70 sequence. Throughout the piece, more soluble amino acids are represented by the higher of the two instrumental voices that speak in each section. The protein sequence is accompanied by the sequence of the encoding DNA, played by harp.
This piece was composed using BankStep sequencing software from Algorithmic Arts, and was created specifically for a student who did a research project on Drosophila heat shock proteins.
The heat shock proteins are widely distributed and a protein very similar to the Drosophila HSP70 is also found in humans. The heat shock proteins are highly conserved, i.e. the amino acid sequence of the protein is very similar even in widely separated species. The sequence for human HSP70 is below: The two proteins are about 50% identical. In addition to amino acid substitutions, there have also been a few additions and deletions of amino acids to the human sequence relative to the Drosophila sequence. The sequence below is aligned for easy comparison. Sections of the human protein in which the number of amino acids is different from that in the fly protein are underlined. Apart from these few "bumps" the sequences can be easily aligned.
Heat Shock Protein 70
Human SequenceMSKGPA[VGID]LGTT[YSCVGVFQ]{HG}[KVEI]IAN{DQ}GNRT
[TP]SY[VAF]TDTE[RLI]{G}
(DAAKN)
QVAM{NPTN}[TV]FD
(AKRL)
{IG}RRFDD
(AVVQSDM)
{KH}WPF[MVVND]{AG}[RPKVQVEY]{KG}[ETKSFY]
(PEEVSSMVLTKMKEIAEAYL)
GKTVT[NAVVTV]P{AY}FN
(DSQRQATKDAGTI)
{AG}L[NVLRIIN]
(EPTAAAIA)
{YGLD}KKVGA[ERNVLIFDL]GGGT
(FDVSILTIED)
{G}_IFEVK[STAGD]{THLG}
(GEDFDNRMVNHFIAEFKRK)
HKKDI{SE}N
(KRAVRRLRTACERAKRT)
[LSS]ST[QASIEI]{DSL}Y{EG}ID[FYTSIT]
(RARFEELNADLFRG){T}(LDPVEKALRD)
{AK}LDKSQIH[DIVLV]GGSTRI
(PKIQKLLQDF)
{FNG}KELNKSIN{PDE}
(AVAYGAAVQAAIL){SG}DKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYS
DNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDA
NGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQ
RDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDK
NQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPS
GGASSGPTIEEVD
More Information on Heat Shock Proteins
http://www.tulane.edu/~biochem/med/hsp.htm
http://www.cryst.bbk.ac.uk/~ubcg16z/hsplec.html
http://pps98.cryst.bbk.ac.uk/assignment/projects/johnston/hsp70a~1.htm