Disease relevance of hslV

• Further characterisation of pHL1 revealed that resistance to nitrofurantoin was due to the overexpression of the hslV-hslU operon which encodes an ATP-dependent protease complex in E. coli [1].
• This is the first molecular study on hslV and hslU in a Leptospira species [2].

High impact information on hslV

• One such locus was identified and shown to carry the recently sequenced hslV hslU (clpQ clpY) operon [3].
• We found several exceptions to this paradigm: (1) Protista: in addition to the 20S proteasome, Leishmania, Trypanosoma and Plasmodium contained hslV, which may have been acquired from an alpha-proteobacterial progenitor of mitochondria [4].
• While either lon, lon clpY, or lon clpQ mutants are UV sensitive at low temperatures, at elevated temperatures the lon mutant loses its UV sensitivity, while the double mutants do not [5].
• This later result was in sharp contrast to those in Escherichia coli, where either lon or hslUV single mutants are strongly impaired in their degradation of puromycyl peptides (hslV is a prcB homologue) [6].
• The hslV gene has an open reading frame (ORF) of 543 bp coding for a 180-amino acid polypeptide (19.476 kD) with 49-62% identity to other bacterial HslV homologs [2].

Biological context of hslV

• PCR genome walking identifies a genetic locus comprising two heat shock genes (hslV and hslU) from Leptospira borgpetersenii serovar hardjobovis [2].

Analytical, diagnostic and therapeutic context of hslV

• PCR walking on genomic DNA of Leptospira borgpetersenii serovar hardjobovis has identified a genetic locus comprising two heat shock genes (hslV and hslU) [2].

References