High impact information on HRB1

• The export of a novel hnRNP-like protein, Hrb1p, which does not bind poly(A)+ RNA, however, is not affected by the lack of methylation [1].
• Consistent with these findings, Gbp2 and Hrb1 associate with actively transcribed genes throughout their entire lengths [2].
• We conclude that recruitment of the SR-like proteins Gbp2 and Hrb1 to mRNA occurs cotranscriptionally by means of association with the TREX complex and/or Ctk1 [2].
• Hrb1 is nuclear at steady state and its import is mediated by the karyopherin Mtr10 [3].
• Here, we present the characterization of Hrb1, a novel component of the transported ribonucleoprotein complex in Saccharomyces cerevisiae [3].

Biological context of HRB1

• TOM34 codes for a putative RNA binding protein, and DOM34 defines a hypothetical polypeptide of 35 kDa, with no significant homology to known proteins [4].
• Cellular localization and phosphorylation of Hrb1p is independent of Sky1p [5].
• Furthermore, we demonstrate that Hrb1p and additional putative Sky1p substrates, identified by computational approach, are not involved in mediating the spermine tolerant phenotype of sky1Delta cells [5].

Analytical, diagnostic and therapeutic context of HRB1

• By using an RNA immunoprecipitation assay, we show that Gbp2 and Hrb1 also are bound to transcripts that are derived from these genes [2].

References