Multifunctional activities of human fibroblast 34-kDa hyaluronic acid-binding protein.
We have already reported that human fibroblast 34-kDa hyaluronic acid-binding protein (HABP) is identical with P32, the protein co-purified with splicing factor SF-2 [Deb and Datta (1996) J. Biol. Chem. 271, 2206-2212]. Data search further revealed that it has 92% sequence homology with a murine protein YL2 which interacts with HIV1 Rev. In this paper we have successfully demonstrated that HIV1 Rev binds with labeled 34-kDa HABP which can be competed with excess unlabeled HABP, suggesting this protein can be a cellular factor promoting HIV1 Rev to function. Interestingly, the multifunctional nature of HABP has been elucidated as it has 100% homology with another protein gC1q, the complement protein. The distinct non-overlapping binding motifs for HA and gC1q have been identified in the same protein, suggesting that either the protein can function independently or its activity is regulated by ligand binding, wherein its binding to one of the ligands may modulate the receptor activity of the other ligand.
Das
S
S
Biochemistry Laboratory, School of Environmental Sciences, Jawaharlal Nehru University, New Delhi, India.
Deb
T B
TB
Kumar
R
R
Datta
K
K
D000595:Amino Acid Sequence; D005347:Fibroblasts / Q000378:metabolism; D015694:Gene Products, rev / Q000378:metabolism; D006801:Humans; D018960:Hyaluronan Receptors / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D015694:Gene Products, rev; D018960:Hyaluronan Receptors; D011994:Recombinant Proteins